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3TXZ

OYE1-W116Q complexed with R-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 Residues20
DetailsBINDING SITE FOR RESIDUE FMN A 401
ChainResidue
APRO34
AGLY324
AASN325
AGLY347
AARG348
APHE374
ATYR375
A07V402
AHOH513
AHOH528
AHOH605
APRO35
AHOH608
ALEU36
ATHR37
AGLY72
AGLN114
AHIS191
AASN194
AARG243

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 07V A 402
ChainResidue
ATHR37
AMET39
ATYR82
AHIS191
AASN194
ATYR196
ATYR375
AFMN401

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
AHOH713
AHOH714
AHOH715
AHOH716
AHOH717
AHOH767

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

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PDB entries from 2024-06-12

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