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3V9I

Crystal structure of human 1-pyrroline-5-carboxylate dehydrogenase mutant S352L

Functional Information from GO Data
ChainGOidnamespacecontents
A0003842molecular_function1-pyrroline-5-carboxylate dehydrogenase activity
A0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006560biological_processproline metabolic process
A0006562biological_processproline catabolic process
A0009055molecular_functionelectron transfer activity
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
A0019470biological_process4-hydroxyproline catabolic process
A0042802molecular_functionidentical protein binding
B0003842molecular_function1-pyrroline-5-carboxylate dehydrogenase activity
B0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0006560biological_processproline metabolic process
B0006562biological_processproline catabolic process
B0009055molecular_functionelectron transfer activity
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
B0019470biological_process4-hydroxyproline catabolic process
B0042802molecular_functionidentical protein binding
C0003842molecular_function1-pyrroline-5-carboxylate dehydrogenase activity
C0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
C0005515molecular_functionprotein binding
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0005829cellular_componentcytosol
C0006560biological_processproline metabolic process
C0006562biological_processproline catabolic process
C0009055molecular_functionelectron transfer activity
C0010133biological_processproline catabolic process to glutamate
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0019470biological_process4-hydroxyproline catabolic process
C0042802molecular_functionidentical protein binding
D0003842molecular_function1-pyrroline-5-carboxylate dehydrogenase activity
D0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
D0005515molecular_functionprotein binding
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0005829cellular_componentcytosol
D0006560biological_processproline metabolic process
D0006562biological_processproline catabolic process
D0009055molecular_functionelectron transfer activity
D0010133biological_processproline catabolic process to glutamate
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0019470biological_process4-hydroxyproline catabolic process
D0042802molecular_functionidentical protein binding
Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GECGGKNF
ChainResidueDetails
AGLY313-PHE320

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008
ChainResidueDetails
AGLU314
BGLU314
CGLU314
DGLU314

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008, ECO:0000269|PubMed:22516612
ChainResidueDetails
ACYS348
BCYS348
CCYS348
DCYS348

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER208
BSER513
CSER208
CLYS233
CGLY286
CGLU447
CSER513
DSER208
DLYS233
DGLY286
DGLU447
ALYS233
DSER513
AGLY286
AGLU447
ASER513
BSER208
BLYS233
BGLY286
BGLU447

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASN211
BASN211
CASN211
DASN211

site_idSWS_FT_FI5
Number of Residues12
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8CHT0
ChainResidueDetails
ALYS31
DLYS31
DLYS347
DLYS395
ALYS347
ALYS395
BLYS31
BLYS347
BLYS395
CLYS31
CLYS347
CLYS395

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER44
BSER44
CSER44
DSER44

site_idSWS_FT_FI7
Number of Residues28
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8CHT0
ChainResidueDetails
ALYS52
BLYS365
BLYS376
BLYS462
BLYS531
BLYS552
CLYS52
CLYS318
CLYS365
CLYS376
CLYS462
ALYS318
CLYS531
CLYS552
DLYS52
DLYS318
DLYS365
DLYS376
DLYS462
DLYS531
DLYS552
ALYS365
ALYS376
ALYS462
ALYS531
ALYS552
BLYS52
BLYS318

site_idSWS_FT_FI8
Number of Residues24
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q8CHT0
ChainResidueDetails
ALYS93
BLYS130
BLYS175
BLYS509
CLYS93
CLYS99
CLYS114
CLYS130
CLYS175
CLYS509
DLYS93
ALYS99
DLYS99
DLYS114
DLYS130
DLYS175
DLYS509
ALYS114
ALYS130
ALYS175
ALYS509
BLYS93
BLYS99
BLYS114

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PDB entries from 2024-10-30

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