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4GE8

OYE1-W116I complexed with (s)-Carvone

Functional Information from GO Data
ChainGOidnamespacecontents
A0003959molecular_functionNADPH dehydrogenase activity
A0005829cellular_componentcytosol
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0018548molecular_functionpentaerythritol trinitrate reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AHOH836
AHOH900
AHOH918
AHOH919
AHOH937
AHOH938

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 402
ChainResidue
AASP83
AASN126

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 403
ChainResidue
ALYS368
AHOH916
AHOH950
ALYS4

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 404
ChainResidue
AALA145

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 405
ChainResidue
ATYR375
A1PE409
AHOH838

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 406
ChainResidue
AALA10
A1PE410

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 407
ChainResidue
ATRP52
A1PE408
AHOH826

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 1PE A 408
ChainResidue
ATRP52
AASP358
AALA379
AGLU389
ANA407
AHOH962

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PE A 409
ChainResidue
ATYR82
APHE123
APHE296
ANA405
AHOH752

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 1PE A 410
ChainResidue
APRO8
AGLN9
AALA10
AHIS43
AASP83
AASN84
AARG334
ALYS362
AGLY363
ANA406
AHOH652
AHOH858

site_idBC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN A 411
ChainResidue
APRO34
APRO35
ALEU36
ATHR37
AGLY72
AGLN114
AHIS191
AASN194
AARG243
AGLY324
AASN325
AGLY347
AARG348
APHE374
A0WU414
AHOH503
AHOH504
AHOH506
AHOH515

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 412
ChainResidue
A1PE413

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PE A 413
ChainResidue
AASP370
AHIS380
AASP384
ANA412
AHOH785

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 0WU A 414
ChainResidue
ATHR37
ATYR82
AILE116
AHIS191
AASN194
ATYR196
ATYR375
AFMN411

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:9830020
ChainResidueDetails
ATYR196

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11668181, ECO:0000269|PubMed:7881908, ECO:0000269|PubMed:9830019
ChainResidueDetails
ATHR37
AGLN114
AARG243
AARG348

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11668181, ECO:0000269|PubMed:7881908
ChainResidueDetails
AHIS191
AASN194
ATYR375

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 319
ChainResidueDetails
ATHR37electrostatic stabiliser, hydrogen bond donor
AHIS191electrostatic stabiliser, hydrogen bond donor
AASN194electrostatic stabiliser, hydrogen bond donor
ATYR196electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASN251hydrogen bond donor, increase acidity

220113

PDB entries from 2024-05-22

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