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6OXD

Structure of Mycobacterium tuberculosis methylmalonyl-CoA mutase with adenosyl cobalamin

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004494molecular_functionmethylmalonyl-CoA mutase activity
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0016853molecular_functionisomerase activity
A0016866molecular_functionintramolecular transferase activity
A0019678biological_processpropionate metabolic process, methylmalonyl pathway
A0031419molecular_functioncobalamin binding
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004494molecular_functionmethylmalonyl-CoA mutase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0009274cellular_componentpeptidoglycan-based cell wall
B0016853molecular_functionisomerase activity
B0016866molecular_functionintramolecular transferase activity
B0019652biological_processlactate fermentation to propionate and acetate
B0019678biological_processpropionate metabolic process, methylmalonyl pathway
B0031419molecular_functioncobalamin binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues43
Detailsbinding site for residue B12 A 1000
ChainResidue
ATYR105
AGLY349
ATRP350
ALEU352
AGLU386
AALA387
AALA389
ALEU390
AGLN470
AGLY628
AHIS629
APHE133
AASP630
AARG631
AGLY632
AGLY672
ASER674
ALEU676
AALA678
AGLY704
AGLY705
APHE724
ALEU135
APRO725
APRO726
ATHR728
A5AD1001
ANJS1002
AHOH1213
AHOH1219
AHOH1228
AHOH1233
AHOH1317
AHIS138
AHOH1323
AHOH1343
AHOH1359
AHOH1376
AALA155
AVAL222
AARG223
ATHR225
AGLU263

site_idAC2
Number of Residues5
Detailsbinding site for residue K A 1003
ChainResidue
ATHR137
ATYR141
AILE159
AASP160
AHOH1175

site_idAC3
Number of Residues49
Detailsbinding site for residues 5AD A 1001 and NJS A 1002
ChainResidue
ATYR91
ATHR93
AMET94
AASN97
AGLN98
ATHR101
AARG103
ATYR105
AGLY107
AALA132
AALA155
ASER180
ATHR182
ATHR211
AGLN213
AARG223
AASN252
ATYR259
AHIS260
AARG299
ASER301
APHE303
AARG342
ATHR343
AHIS344
AGLN346
AGLN377
ASER378
AASN382
AGLU386
ALEU390
APRO391
AB121000
AHOH1117
AHOH1144
AHOH1145
AHOH1168
AHOH1174
AHOH1210
AHOH1211
AHOH1212
AHOH1273
AHOH1282
AHOH1301
AHOH1321
AHOH1329
AHOH1339
AHOH1388
AHOH1389

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues12
DetailsLIPOCALIN Lipocalin signature. DLE..QVRGRWRNA
ChainResidueDetails
BASP11-ALA22

site_idPS00544
Number of Residues26
DetailsMETMALONYL_COA_MUTASE Methylmalonyl-CoA mutase signature. RIARNTqlLLlEEshvgRvlDPaGGS
ChainResidueDetails
BARG365-SER390
AARG397-SER422

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues25
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P11653
ChainResidueDetails
ATYR91
AGLN213
AVAL222
AARG223
AHIS260
AARG299
ASER301
AGLY349
AGLU386
AALA389
AGLY628
AMET94
AASP630
AARG631
ASER674
ALEU676
AGLY705
ATHR728
ATHR101
AARG103
ATYR105
ASER130
APHE133
AALA155
ATHR211

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000250|UniProtKB:P11653
ChainResidueDetails
AHIS629

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P11653
ChainResidueDetails
ATYR105

218853

PDB entries from 2024-04-24

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