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1MO9

NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE COMPLEXED WITH 2-KETOPROPYL COENZYME M

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0042208biological_processpropylene catabolic process
A0050628molecular_function2-oxopropyl-CoM reductase (carboxylating) activity
B0016491molecular_functionoxidoreductase activity
B0042208biological_processpropylene catabolic process
B0050628molecular_function2-oxopropyl-CoM reductase (carboxylating) activity
Functional Information from PDB Data
site_idAC1
Number of Residues37
DetailsBINDING SITE FOR RESIDUE FAD A 1013
ChainResidue
AGLY50
AALA86
ACYS87
AHIS90
AHIS91
AALA158
AALA181
AVAL182
AGLY183
AHIS202
ATHR225
AGLY52
ATYR229
AGLY352
AASP353
AMET359
AGLU360
AMET361
AALA364
AHOH1017
AHOH1018
AHOH1028
AALA53
AHOH1059
AHOH1066
AHOH1131
AHOH1165
AHOH1192
AHOH1401
BPHE501
BHOH1025
AALA54
AASP73
AARG74
ATRP75
AGLY80
ASER81

site_idAC2
Number of Residues38
DetailsBINDING SITE FOR RESIDUE FAD B 1014
ChainResidue
APHE501
AHOH1029
BGLY50
BGLY52
BALA53
BALA54
BVAL72
BASP73
BARG74
BTRP75
BGLY80
BSER81
BALA86
BCYS87
BHIS90
BHIS91
BPRO157
BALA158
BALA181
BVAL182
BGLY183
BHIS202
BTYR229
BGLY352
BASP353
BMET359
BGLU360
BMET361
BALA364
BPHE390
BHOH1048
BHOH1061
BHOH1065
BHOH1074
BHOH1081
BHOH1100
BHOH1321
BHOH1358

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE KPC A 1015
ChainResidue
AALA53
AARG56
APHE57
AGLY79
APRO83
APRO136
AMET140
AMET361
AARG365
AHOH1127
AHOH1169

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE KPC B 1016
ChainResidue
BARG56
BPHE57
BGLY79
BPRO83
BPRO136
BMET140
BMET361
BARG365
BHOH1119
BHOH1159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:12390015, ECO:0000269|PubMed:16388586, ECO:0000269|PubMed:21192936, ECO:0007744|PDB:1MO9, ECO:0007744|PDB:1MOK, ECO:0007744|PDB:2C3C, ECO:0007744|PDB:2C3D, ECO:0007744|PDB:3Q6J
ChainResidueDetails
AALA53
BASP353
BMET361
BPHE501
ASER81
AALA158
AASP353
AMET361
APHE501
BALA53
BSER81
BALA158

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12390015, ECO:0000269|PubMed:21192936, ECO:0000305|PubMed:16388586, ECO:0007744|PDB:1MO9, ECO:0007744|PDB:3Q6J
ChainResidueDetails
AARG56
AARG365
BARG56
BARG365

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21192936, ECO:0000305|PubMed:16388586, ECO:0007744|PDB:3Q6J
ChainResidueDetails
ACYS82
BCYS82

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16388586, ECO:0000269|PubMed:21192936, ECO:0007744|PDB:2C3C, ECO:0007744|PDB:3Q6J
ChainResidueDetails
AGLY222
AARG245
AGLU360
BGLY222
BARG245
BGLU360

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS87
ACYS82

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BCYS87
BCYS82

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS87
AHIS137
ACYS82
ALEU78
APHE501

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BCYS87
BHIS137
BCYS82
BLEU78
BPHE501

site_idMCSA1
Number of Residues5
DetailsM-CSA 378
ChainResidueDetails
ALEU78electrostatic stabiliser, modifies pKa
ACYS82covalent catalysis
ACYS87covalent catalysis
AHIS137modifies pKa
APHE501electrostatic stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 378
ChainResidueDetails
BLEU78electrostatic stabiliser, modifies pKa
BCYS82covalent catalysis
BCYS87covalent catalysis
BHIS137modifies pKa
BPHE501electrostatic stabiliser

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PDB entries from 2024-07-10

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