Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T15569 | Target Info | |||
| Target Name | Methylmalonyl-CoA mutase (MMUT) | ||||
| Synonyms | Methylmalonyl-CoA isomerase; MUT; MCM | ||||
| Target Type | Successful Target | ||||
| Gene Name | MUT | ||||
| Biochemical Class | Intramolecular transferases | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Cobalamin | Ligand Info | |||
| Canonical SMILES | CC1=CC2=C(C=C1C)N(C=N2)C3C(C(C(O3)CO)OP(=O)([O-])OC(C)CNC(=O)CCC4(C(C5C6(C(C(C(=N6)C(=C7C(C(C(=N7)C=C8C(C(C(=N8)C(=C4[N-]5)C)CCC(=O)N)(C)C)CCC(=O)N)(C)CC(=O)N)C)CCC(=O)N)(C)CC(=O)N)C)CC(=O)N)C)O.[C-]#N.[Co+3] | ||||
| InChI | 1S/C62H90N13O14P.CN.Co/c1-29-20-39-40(21-30(29)2)75(28-70-39)57-52(84)53(41(27-76)87-57)89-90(85,86)88-31(3)26-69-49(83)18-19-59(8)37(22-46(66)80)56-62(11)61(10,25-48(68)82)36(14-17-45(65)79)51(74-62)33(5)55-60(9,24-47(67)81)34(12-15-43(63)77)38(71-55)23-42-58(6,7)35(13-16-44(64)78)50(72-42)32(4)54(59)73-56;1-2;/h20-21,23,28,31,34-37,41,52-53,56-57,76,84H,12-19,22,24-27H2,1-11H3,(H15,63,64,65,66,67,68,69,71,72,73,74,77,78,79,80,81,82,83,85,86);;/q;-1;+3/p-2/t31-,34-,35-,36-,37+,41-,52-,53-,56-,57+,59-,60+,61+,62+;;/m1../s1 | ||||
| InChIKey | FDJOLVPMNUYSCM-WZHZPDAFSA-L | ||||
| PubChem Compound ID | 46853873 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 2XIJ Crystal structure of human methylmalonyl-CoA mutase in complex with adenosylcobalamin | ||||||
| Method | X-ray diffraction | Resolution | 1.95 Å | Mutation | Yes | [1] |
| PDB Sequence |
QQPLHPEWAA
45 LAKKQLKGKN55 PEDLIWHTPE65 GISIKPLYSK75 RDTMDLPEEL85 PGVKPFTRGP 95 YPTMYTFRPW105 TIRQYAGFST115 VEESNKFYKD125 NIKAGQQGLS135 VAFDLATHRG 145 YDSDNPRVRG155 DVGMAGVAID165 TVEDTKILFD175 GIPLEKMSVS185 MTMNGAVIPV 195 LANFIVTGEE205 QGVPKEKLTG215 TIQNDILKEF225 MVRNTYIFPP235 EPSMKIIADI 245 FEYTAKHMPK255 FNSISISGYH265 MQEAGADAIL275 ELAYTLADGL285 EYSRTGLQAG 295 LTIDEFAPRL305 SFFWGIGMNF315 YMEIAKMRAG325 RRLWAHLIEK335 MFQPKNSKSL 345 LLRAHCQTSG355 WSLTEQDPYN365 NIVRTAIEAM375 AAVFGGTQSL385 HTNSFDEALG 395 LPTVKSARIA405 RNTQIIIQEE415 SGIPKVADPW425 GGSYMMECLT435 NDVYDAALKL 445 INEIEEMGGM455 AKAVAEGIPK465 LRIEECAARR475 QARIDSGSEV485 IVGVNKYQLE 495 KEDTVEVLAI505 DNTSVRNRQI515 EKLKKIKSSR525 DQALAERCLA535 ALTECAASGD 545 GNILALAVDA555 SRARCTVGEI565 TDALKKVFGE575 HKANDRMVSG585 AYRQEFGESK 595 EITSAIKRVH605 KFMEREGRRP615 RLLVAKMGQD625 GHDRGAKVIA635 TGFADLGFDV 645 DIGPLFQTPR655 EVAQQAVDAD665 VHAVGVSTLA675 AGHKTLVPEL685 IKELNSLGRP 695 DILVMCGGVI705 PPQDYEFLFE715 VGVSNVFGPG725 TRIPKAAVQV735 LDDIEKCLEK 745
|
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|
|
PHE138
3.601
LEU140
3.679
HIS143
3.592
ALA160
3.172
GLY161
4.875
VAL227
2.758
ARG228
2.767
ASN229
4.192
THR230
3.400
TYR264
4.505
HIS265
4.070
GLU268
3.388
ALA269
3.838
GLY355
3.751
TRP356
3.575
LEU358
4.930
GLU392
3.004
ALA393
3.006
LEU394
3.362
GLY395
2.870
LEU396
4.706
LYS465
4.824
GLN476
3.542
LEU617
4.409
VAL619
4.601
GLN624
4.383
ASP625
3.782
GLY626
2.831
HIS627
2.132
ASP628
2.737
ARG629
3.059
GLY630
3.366
ALA631
4.490
VAL633
4.149
ILE634
3.511
PHE638
3.935
GLY670
3.558
VAL671
4.307
SER672
2.677
LEU674
3.474
ALA675
3.542
ALA676
3.676
MET700
4.915
GLY702
3.575
GLY703
3.056
VAL704
3.395
PHE722
3.452
GLY723
3.310
PRO724
3.622
GLY725
3.930
THR726
2.579
ARG727
4.695
ALA731
4.494
VAL735
4.353
|
|||||
| PDB ID: 2XIQ Crystal structure of human methylmalonyl-CoA mutase in complex with adenosylcobalamin and malonyl-CoA | ||||||
| Method | X-ray diffraction | Resolution | 1.95 Å | Mutation | No | [1] |
| PDB Sequence |
QQPLHPEWAA
45 LAKKQLKGKN55 PEDLIWHTPE65 GISIKPLYSK75 RDTMDLPEEL85 PGVKPFTRGP 95 YPTMYTFRPW105 TIRQYAGFST115 VEESNKFYKD125 NIKAGQQGLS135 VAFDLATHRG 145 YDSDNPRVRG155 DVGMAGVAID165 TVEDTKILFD175 GIPLEKMSVS185 MTMNGAVIPV 195 LANFIVTGEE205 QGVPKEKLTG215 TIQNDILKEF225 MVRNTYIFPP235 EPSMKIIADI 245 FEYTAKHMPK255 FNSISISGYH265 MQEAGADAIL275 ELAYTLADGL285 EYSRTGLQAG 295 LTIDEFAPRL305 SFFWGIGMNF315 YMEIAKMRAG325 RRLWAHLIEK335 MFQPKNSKSL 345 LLRAHCQTSG355 WSLTEQDPYN365 NIVRTAIEAM375 AAVFGGTQSL385 HTNSFDEALG 395 LPTVKSARIA405 RNTQIIIQEE415 SGIPKVADPW425 GGSYMMECLT435 NDVYDAALKL 445 INEIEEMGGM455 AKAVAEGIPK465 LRIEECAARR475 QARIDSGSEV485 IVGVNKYQLE 495 KEDTVEVLAI505 DNTSVRNRQI515 EKLKKIKSSR525 DQALAERCLA535 ALTECAASGD 545 GNILALAVDA555 SRARCTVGEI565 TDALKKVFGE575 HKANDRMVSG585 AYRQEFGESK 595 EITSAIKRVH605 KFMEREGRRP615 RLLVAKMGQD625 GHDRGAKVIA635 TGFADLGFDV 645 DIGPLFQTPR655 EVAQQAVDAD665 VHAVGVSTLA675 AGHKTLVPEL685 IKELNSLGRP 695 DILVMCGGVI705 PPQDYEFLFE715 VGVSNVFGPG725 TRIPKAAVQV735 LDDIEKCLEK 745 KQQS
|
|||||
|
|
TYR110
3.017
ALA137
4.154
PHE138
2.858
ASP139
4.876
LEU140
3.379
HIS143
2.976
MET159
4.817
ALA160
2.813
GLY161
4.222
THR187
4.995
VAL227
2.892
ARG228
2.731
ASN229
4.458
THR230
3.504
TYR264
3.547
HIS265
3.657
GLU268
3.610
ALA269
4.031
GLY355
3.137
TRP356
3.276
LEU358
3.423
ASP391
4.419
GLU392
2.854
ALA393
3.811
LEU394
4.370
GLY395
2.800
LEU396
3.594
PRO397
4.856
GLN476
3.461
LEU617
4.300
VAL619
4.536
GLN624
4.345
ASP625
3.787
GLY626
2.766
HIS627
2.480
ASP628
2.859
ARG629
2.895
GLY630
3.328
ALA631
4.653
VAL633
4.046
ILE634
3.634
PHE638
3.843
GLY670
3.504
VAL671
4.272
SER672
2.770
THR673
4.932
LEU674
2.902
ALA675
3.832
ALA676
3.500
GLY702
3.433
GLY703
2.883
VAL704
3.443
PHE722
3.164
GLY723
3.308
PRO724
3.672
GLY725
4.037
THR726
2.646
ARG727
4.798
ALA731
4.373
VAL735
4.209
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation. J Biol Chem. 2010 Dec 3;285(49):38204-13. | ||||
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