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1YBV

STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND AN ACTIVE SITE INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0005575cellular_componentcellular_component
A0016491molecular_functionoxidoreductase activity
A0042438biological_processmelanin biosynthetic process
A0047039molecular_functiontetrahydroxynaphthalene reductase activity
B0005575cellular_componentcellular_component
B0016491molecular_functionoxidoreductase activity
B0042438biological_processmelanin biosynthetic process
B0047039molecular_functiontetrahydroxynaphthalene reductase activity
Functional Information from PDB Data
site_idA1
Number of Residues11
DetailsCATALYTIC SITE.
ChainResidue
AVAL118
ATRP243
AMET283
ASER164
AILE165
ATYR178
AGLY210
AMET215
AVAL219
ACYS220
ATYR223

site_idA2
Number of Residues12
DetailsCOFACTOR BINDING SITE.
ChainResidue
AARG39
AILE41
AALA61
AASN62
ASER63
AVAL88
AASN114
ASER115
ATYR178
ALYS182
AILE211
ATHR213

site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NDP A 284
ChainResidue
AGLY36
AARG39
AGLY40
AILE41
AALA61
AASN62
ASER63
AALA86
AASN87
AVAL88
AASN114
ASER115
AGLY116
AMET162
AGLY163
ASER164
ATYR178
ALYS182
APRO208
AGLY210
AILE211
ATHR213
AMET215
ABEA285

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BEA A 285
ChainResidue
ASER164
AILE165
ATYR178
AGLY210
AMET215
ATYR223
ANDP284

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NDP B 284
ChainResidue
BMET215
BBEA285
BGLY36
BARG39
BGLY40
BILE41
BALA61
BASN62
BSER63
BALA86
BASN87
BVAL88
BASN114
BSER115
BGLY116
BMET162
BGLY163
BSER164
BTYR178
BLYS182
BPRO208
BGLY210
BILE211
BTHR213

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BEA B 285
ChainResidue
BSER164
BILE165
BTYR178
BGLY210
BMET215
BTYR223
BNDP284

site_idB1
Number of Residues11
DetailsCATALYTIC SITE.
ChainResidue
BVAL118
BSER164
BILE165
BTYR178
BGLY210
BMET215
BVAL219
BCYS220
BTYR223
BTRP243
BMET283

site_idB2
Number of Residues12
DetailsCOFACTOR BINDING SITE.
ChainResidue
BARG39
BILE41
BALA61
BASN62
BSER63
BVAL88
BASN114
BSER115
BTYR178
BLYS182
BILE211
BTHR213

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. ItgqakavpkHavYSGSKGAIeTFArCMA
ChainResidueDetails
AILE165-ALA193

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:11342131, ECO:0000269|PubMed:8939741
ChainResidueDetails
ASER179
BSER179

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11342131, ECO:0000269|PubMed:8939741
ChainResidueDetails
AGLY40
BGLY40

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AILE165
BILE165

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 12604210
ChainResidueDetails
AASN138
ASER164
ALYS182
ATYR178

site_idCSA2
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 12604210
ChainResidueDetails
BASN138
BSER164
BLYS182
BTYR178

site_idMCSA1
Number of Residues4
DetailsM-CSA 891
ChainResidueDetails
AILE165electrostatic stabiliser
ASER179proton acceptor, proton donor, proton relay
AGLY183electrostatic stabiliser, proton acceptor, proton donor, proton relay
AILE224electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 891
ChainResidueDetails
BILE165electrostatic stabiliser
BSER179proton acceptor, proton donor, proton relay
BGLY183electrostatic stabiliser, proton acceptor, proton donor, proton relay
BILE224electrostatic stabiliser

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PDB entries from 2024-08-07

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