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4H6K

W116I mutant of OYE1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003959molecular_functionNADPH dehydrogenase activity
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
ATYR346
AGLY347
AARG348
APHE374
ATYR375
AHOH503
AHOH519
AHOH528
APRO35
AHOH637
ALEU36
ATHR37
AGLY72
AGLN114
AHIS191
AASN194
AARG243

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

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
AHOH569
AHOH586
AHOH649
AHOH657
AHOH658
AHOH768

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 1PE A 404
ChainResidue
AASP370
AHIS380
AASP384
AHOH600

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 1PE A 405
ChainResidue
ATHR58
AGLN62
ALYS107
AHOH574

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 2024-07-24

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