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

2GR9

Crystal structure of P5CR complexed with NADH

Functional Information from GO Data
ChainGOidnamespacecontents
A0004735molecular_functionpyrroline-5-carboxylate reductase activity
A0006561biological_processproline biosynthetic process
B0004735molecular_functionpyrroline-5-carboxylate reductase activity
B0006561biological_processproline biosynthetic process
C0004735molecular_functionpyrroline-5-carboxylate reductase activity
C0006561biological_processproline biosynthetic process
D0004735molecular_functionpyrroline-5-carboxylate reductase activity
D0006561biological_processproline biosynthetic process
E0004735molecular_functionpyrroline-5-carboxylate reductase activity
E0006561biological_processproline biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NAI A 1300
ChainResidue
AARG129
AHOH1412
AHOH1431
AHOH1435
CARG204
CGLN208
CHOH3395
AGLU130
ASER154
AGLY157
APHE158
ALEU218
AHIS219
AGLU1301
AHOH1408

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GLU A 1301
ChainResidue
ANAI1300
AHOH1401
AHOH1408
AHOH1429

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NAI B 2300
ChainResidue
BARG129
BGLU130
BSER154
BSER155
BVAL156
BGLY157
BPHE158
BARG200
BARG204
BGLN208
BLEU211
BLEU218
BHIS219
BGLU2301
BHOH2359
BHOH2377
BHOH2380

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GLU B 2301
ChainResidue
BARG129
BNAI2300

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NAI C 3300
ChainResidue
AARG204
ALEU205
AGLN208
ALEU211
CARG129
CGLU130
CSER154
CSER155
CGLY157
CPHE158
CLEU218
CHIS219
CGLU3301
CHOH3408

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GLU C 3301
ChainResidue
CARG129
CNAI3300

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NAI D 4300
ChainResidue
DGLU130
DSER154
DPHE158
DLYS215
DLEU218
DHIS219
DGLU4301
DHOH4410
DHOH4413
DHOH4416
DHOH4423
DHOH4436
EARG204
EGLN208

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GLU D 4301
ChainResidue
DNAI4300

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NAI E 5300
ChainResidue
DARG204
DGLN208
EGLU130
ESER154
EGLY157
EPHE158
ELEU218
EHIS219
EGLU5301
EHOH5402
EHOH5404

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GLU E 5301
ChainResidue
EHIS219
ENAI5300

Functional Information from PROSITE/UniProt
site_idPS00521
Number of Residues23
DetailsP5CR Delta 1-pyrroline-5-carboxylate reductase signature. Pgq.LkdnVSSpGGaTihALhvLE
ChainResidueDetails
APRO224-GLU246

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues25
DetailsBINDING: BINDING => ECO:0000269|Ref.18
ChainResidueDetails
AILE6
BCYS95
CILE6
CSER34
CASN56
CALA69
CCYS95
DILE6
DSER34
DASN56
DALA69
ASER34
DCYS95
EILE6
ESER34
EASN56
EALA69
ECYS95
AASN56
AALA69
ACYS95
BILE6
BSER34
BASN56
BALA69

site_idSWS_FT_FI2
Number of Residues5
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.8, ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330
ChainResidueDetails
ASER2
BSER2
CSER2
DSER2
ESER2

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon