Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4DC0

Crystal Structure of F189W Actinorhodin Polyketide Ketoreductase with NADPH

Functional Information from GO Data
ChainGOidnamespacecontents
A0008202biological_processsteroid metabolic process
A0016491molecular_functionoxidoreductase activity
A0017000biological_processantibiotic biosynthetic process
B0008202biological_processsteroid metabolic process
B0016491molecular_functionoxidoreductase activity
B0017000biological_processantibiotic biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NDP A 301
ChainResidue
AGLY13
AASP63
AVAL64
AASN90
AILE142
AALA143
ASER144
ATYR157
ALYS161
APRO187
AGLY188
ATHR15
AVAL190
ATHR192
APRO193
AMET194
AHOH401
AHOH404
BARG51
ASER16
AGLY17
AILE18
AALA37
AARG38
AGLY39
ACYS62

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NDP B 301
ChainResidue
BGLY13
BTHR15
BSER16
BILE18
BALA37
BARG38
BGLY39
BCYS62
BASP63
BVAL64
BASN90
BALA91
BGLY92
BALA143
BSER144
BTYR157
BLYS161
BPRO187
BGLY188
BVAL190
BTHR192
BPRO193
BMET194

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 Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15458634, ECO:0000269|PubMed:15544323
ChainResidueDetails
AVAL11
AASP63
ALYS161
BVAL11
BASP63
BLYS161

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER144
BSER144

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon