Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1X7H

Actinorhodin Polyketide Ketoreductase, with NADPH bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0006629biological_processlipid metabolic process
A0008202biological_processsteroid metabolic process
A0016491molecular_functionoxidoreductase activity
A0017000biological_processantibiotic biosynthetic process
A0032787biological_processmonocarboxylic acid metabolic process
B0006629biological_processlipid metabolic process
B0008202biological_processsteroid metabolic process
B0016491molecular_functionoxidoreductase activity
B0017000biological_processantibiotic biosynthetic process
B0032787biological_processmonocarboxylic acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NDP A 301
ChainResidue
AGLY13
AASP63
AVAL64
AASN90
AALA91
AGLY92
AILE142
AALA143
ASER144
ATYR157
ALYS161
ATHR15
APRO187
AGLY188
AVAL190
ATHR192
APRO193
AMET194
AHOH309
AHOH311
AHOH315
AHOH318
ASER16
AHOH334
AHOH431
BARG51
BHOH327
AGLY17
AILE18
AALA37
AARG38
AGLY39
ACYS62

site_idAC2
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NDP B 301
ChainResidue
BGLY13
BTHR15
BSER16
BILE18
BALA37
BARG38
BGLY39
BCYS62
BASP63
BVAL64
BASN90
BALA91
BGLY92
BILE142
BALA143
BSER144
BTYR157
BLYS161
BPRO187
BGLY188
BVAL190
BTHR192
BPRO193
BMET194
BHOH302
BHOH332
BHOH346
BHOH374
BHOH386
BHOH393
BHOH405

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. StggkqgvvhAapYSASKHGVvGFTkALG
ChainResidueDetails
ASER144-GLY172

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR157
BTYR157

site_idSWS_FT_FI2
Number of Residues22
DetailsBINDING: BINDING => ECO:0000269|PubMed:15458634, ECO:0000269|PubMed:15544323, ECO:0007744|PDB:1W4Z, ECO:0007744|PDB:1X7G, ECO:0007744|PDB:1X7H, ECO:0007744|PDB:1XR3
ChainResidueDetails
ATHR15
AVAL190
ATHR192
BTHR15
BSER16
BILE18
BARG38
BGLY39
BASP63
BVAL64
BASN90
ASER16
BLYS161
BVAL190
BTHR192
AILE18
AARG38
AGLY39
AASP63
AVAL64
AASN90
ALYS161

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15458634, ECO:0000269|PubMed:15544323, ECO:0007744|PDB:1X7G, ECO:0007744|PDB:1X7H, ECO:0007744|PDB:1XR3
ChainResidueDetails
ATYR157
BTYR157

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS161
ASER144
ATYR157

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BLYS161
BSER144
BTYR157

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
AASN114
ALYS161
ASER144
ATYR157

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BASN114
BLYS161
BSER144
BTYR157

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
AALA154
ALYS161

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BALA154
BLYS161

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS161
ATYR157

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BLYS161
BTYR157

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon