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

4IQG

Crystal structure of BPRO0239 oxidoreductase from Polaromonas sp. JS666 in NADP bound form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0000166molecular_functionnucleotide binding
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
C0000166molecular_functionnucleotide binding
C0016491molecular_functionoxidoreductase activity
C0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
D0000166molecular_functionnucleotide binding
D0016491molecular_functionoxidoreductase activity
D0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT C 301
ChainResidue
CALA145
CLEU148
CSER150
CPRO151
CARG248

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT C 302
ChainResidue
DTHR238
DGLY239
CASP243
CTHR245
CARG248
DLEU169

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT C 303
ChainResidue
CLYS3
CGLN25

site_idAC4
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NAP C 304
ChainResidue
CGLY9
CSER11
CARG12
CGLY13
CILE14
CASN32
CTYR33
CALA34
CSER35
CASN36
CALA59
CASP60
CVAL61
CASN87
CALA88
CILE111
CVAL141
CSER142
CSER143
CTYR157
CLYS161
CPRO187
CGLY188
CILE190
CTHR192
CILE194
CHIS195
CHOH434
CHOH498
CHOH524

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 301
ChainResidue
ALEU169
ATHR238
AGLY239
BARG147
BASP243
BTHR245
BARG248

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 302
ChainResidue
AARG147
AASP243
ATHR245
AARG248
AHOH404
BTHR238
BGLY239

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
AGLY136
ASER137
AGLY179
AARG181
ALEU230
AGLY231
AASP232
AHOH511

site_idAC8
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAP A 304
ChainResidue
AGLY9
ASER11
AARG12
AGLY13
AILE14
AASN32
ATYR33
AALA34
ASER35
AASN36
AALA59
AASP60
AVAL61
AASN87
AALA88
AILE111
AVAL141
ASER142
ASER143
ATYR157
ALYS161
APRO187
AGLY188
AILE190
AHOH412
AHOH493

site_idAC9
Number of Residues34
DetailsBINDING SITE FOR RESIDUE NAP B 301
ChainResidue
BASN36
BALA59
BASP60
BVAL61
BASN87
BALA88
BGLY89
BVAL141
BSER142
BSER143
BTYR157
BLYS161
BPRO187
BGLY188
BILE190
BTHR192
BILE194
BHIS195
BHOH431
BHOH437
BHOH442
BHOH447
BHOH465
BHOH481
BHOH487
BHOH497
BGLY9
BSER11
BARG12
BGLY13
BILE14
BASN32
BALA34
BSER35

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT B 302
ChainResidue
BSER143
BALA144
BPRO187
BGLY188
BILE189
BARG248

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT B 303
ChainResidue
BGLN25

site_idBC3
Number of Residues35
DetailsBINDING SITE FOR RESIDUE NAP D 301
ChainResidue
DGLY9
DSER11
DARG12
DGLY13
DILE14
DASN32
DTYR33
DALA34
DSER35
DASN36
DALA59
DASP60
DVAL61
DASN87
DALA88
DGLY89
DVAL141
DSER142
DSER143
DTYR157
DLYS161
DPRO187
DGLY188
DILE190
DTHR192
DILE194
DHIS195
DHOH414
DHOH424
DHOH432
DHOH438
DHOH457
DHOH463
DHOH469
DHOH473

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG D 302
ChainResidue
BLYS173
DALA145
DLEU148
DSER150
DARG248

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT D 303
ChainResidue
BGLU174
DARG96

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT D 304
ChainResidue
CLEU169
CTHR238
CGLY239
DARG147
DASP243
DTHR245
DARG248

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. AaarlgspgqYvdYAAAKGAIdTFTlGLA
ChainResidueDetails
CALA144-ALA172

250059

PDB entries from 2026-03-04

PDB statisticsPDBj update infoContact PDBjnumon