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1DOH

STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND 4-NITRO-INDEN-1-ONE

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_idAC1
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NDP A 500
ChainResidue
AGLY36
AVAL88
AASN114
ASER115
AGLY116
AMET162
AGLY163
ASER164
ATYR178
ALYS182
APRO208
AARG39
AGLY209
AGLY210
AILE211
ATHR213
AASP214
AMET215
ANID502
AHOH533
AHOH535
AHOH536
AGLY40
AHOH537
AHOH541
AHOH706
AHOH708
AILE41
AALA61
AASN62
ASER63
AALA86
AASN87

site_idAC2
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NDP B 501
ChainResidue
BGLY36
BARG39
BGLY40
BILE41
BALA61
BASN62
BSER63
BALA86
BASN87
BVAL88
BASN114
BSER115
BGLY116
BMET162
BGLY163
BTYR178
BLYS182
BPRO208
BGLY209
BGLY210
BILE211
BTHR213
BMET215
BNID503
BHOH532
BHOH534
BHOH535
BHOH540
BHOH543
BHOH558
BHOH625

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NID A 502
ChainResidue
ASER164
ATYR178
AGLY210
ATYR216
ACYS220
ATYR223
AMET283
ANDP500

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NID B 503
ChainResidue
BSER164
BTYR178
BGLY210
BMET215
BTYR216
BCYS220
BTYR223
BMET283
BNDP501

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
ATYR178
BTYR178

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11342131, ECO:0000269|PubMed:8939741
ChainResidueDetails
AARG39
BARG39

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ASER164
BSER164

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ASER164
ALYS182
ATYR178

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BSER164
BLYS182
BTYR178

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
AASN138
ASER164
ALYS182
ATYR178

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BASN138
BSER164
BLYS182
BTYR178

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
AHIS175
ALYS182

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BHIS175
BLYS182

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS182
ATYR178

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BLYS182
BTYR178

site_idMCSA1
Number of Residues4
DetailsM-CSA 891
ChainResidueDetails
ASER164electrostatic stabiliser
ATYR178proton acceptor, proton donor, proton relay
ALYS182electrostatic stabiliser, proton acceptor, proton donor, proton relay
ATYR223electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 891
ChainResidueDetails
BSER164electrostatic stabiliser
BTYR178proton acceptor, proton donor, proton relay
BLYS182electrostatic stabiliser, proton acceptor, proton donor, proton relay
BTYR223electrostatic stabiliser

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PDB entries from 2024-09-11

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