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

4K57

Structure of Thermus thermophilus 1-pyrroline-5-carboxylate dehydrogenase R100A mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0003842molecular_function1-pyrroline-5-carboxylate dehydrogenase activity
A0009898cellular_componentcytoplasmic side of plasma membrane
A0010133biological_processproline catabolic process to glutamate
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0003842molecular_function1-pyrroline-5-carboxylate dehydrogenase activity
B0009898cellular_componentcytoplasmic side of plasma membrane
B0010133biological_processproline catabolic process to glutamate
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MRD A 601
ChainResidue
AGLU158
AHOH879
AHOH900
BPHE6
BTYR144
BARG147
BLEU500
BHOH710

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MRD B 601
ChainResidue
ALEU500
AHOH796
BGLU158
BHOH707
BHOH890
ATYR144

Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. YgFQGQKCSAAS
ChainResidueDetails
ATYR315-SER326

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. VETGGKDA
ChainResidueDetails
AVAL287-ALA294

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon