Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3V9H

Crystal structure of human 1-pyrroline-5-carboxylate dehydrogenase mutant S352A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
A	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005829	cellular_component	cytosol
A	0006560	biological_process	proline metabolic process
A	0006562	biological_process	L-proline catabolic process
A	0009055	molecular_function	electron transfer activity
A	0010133	biological_process	L-proline catabolic process to L-glutamate
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0019470	biological_process	trans-4-hydroxy-L-proline catabolic process
A	0042802	molecular_function	identical protein binding
B	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
B	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005829	cellular_component	cytosol
B	0006560	biological_process	proline metabolic process
B	0006562	biological_process	L-proline catabolic process
B	0009055	molecular_function	electron transfer activity
B	0010133	biological_process	L-proline catabolic process to L-glutamate
B	0016491	molecular_function	oxidoreductase activity
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0019470	biological_process	trans-4-hydroxy-L-proline catabolic process
B	0042802	molecular_function	identical protein binding
C	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
C	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0005829	cellular_component	cytosol
C	0006560	biological_process	proline metabolic process
C	0006562	biological_process	L-proline catabolic process
C	0009055	molecular_function	electron transfer activity
C	0010133	biological_process	L-proline catabolic process to L-glutamate
C	0016491	molecular_function	oxidoreductase activity
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0019470	biological_process	trans-4-hydroxy-L-proline catabolic process
C	0042802	molecular_function	identical protein binding
D	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
D	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0005829	cellular_component	cytosol
D	0006560	biological_process	proline metabolic process
D	0006562	biological_process	L-proline catabolic process
D	0009055	molecular_function	electron transfer activity
D	0010133	biological_process	L-proline catabolic process to L-glutamate
D	0016491	molecular_function	oxidoreductase activity
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0019470	biological_process	trans-4-hydroxy-L-proline catabolic process
D	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 564

Chain	Residue
A	LYS233
A	SER235
A	ASP236

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 565

Chain	Residue
A	SER349
A	GLY512
A	SER513
A	PHE520
A	HOH580

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 564

Chain	Residue
B	GLY512
B	SER513
B	PHE520
B	SER349

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 564

Chain	Residue
C	SER349
C	THR511
C	GLY512
C	SER513
C	PHE520

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 564

Chain	Residue
D	GLU165
D	SER349
D	THR511
D	GLY512
D	SER513
D	PHE520

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 565

Chain	Residue
B	ARG47
B	GLN51

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 C 565

Chain	Residue
C	ARG47

Functional Information from PROSITE/UniProt

site_id	PS00070
Number of Residues	12
Details	ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FeYGGQKCSACA

Chain	Residue	Details
A	PHE341-ALA352

site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GECGGKNF

Chain	Residue	Details
A	GLY313-PHE320

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU10007, ECO:0000255\|PROSITE-ProRule:PRU10008

Chain	Residue	Details
A	GLU314
B	GLU314
C	GLU314
D	GLU314

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000255\|PROSITE-ProRule:PRU10007, ECO:0000255\|PROSITE-ProRule:PRU10008, ECO:0000269\|PubMed:22516612

Chain	Residue	Details
A	CYS348
B	CYS348
C	CYS348
D	CYS348

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	SER208
B	SER513
C	SER208
C	LYS233
C	GLY286
C	GLU447
C	SER513
D	SER208
D	LYS233
D	GLY286
D	GLU447
A	LYS233
D	SER513
A	GLY286
A	GLU447
A	SER513
B	SER208
B	LYS233
B	GLY286
B	GLU447

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000250

Chain	Residue	Details
A	ASN211
B	ASN211
C	ASN211
D	ASN211

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:Q8CHT0

Chain	Residue	Details
A	LYS31
D	LYS31
D	LYS347
D	LYS395
A	LYS347
A	LYS395
B	LYS31
B	LYS347
B	LYS395
C	LYS31
C	LYS347
C	LYS395

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER44
B	SER44
C	SER44
D	SER44

site_id	SWS_FT_FI7
Number of Residues	28
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q8CHT0

Chain	Residue	Details
A	LYS52
B	LYS365
B	LYS376
B	LYS462
B	LYS531
B	LYS552
C	LYS52
C	LYS318
C	LYS365
C	LYS376
C	LYS462
A	LYS318
C	LYS531
C	LYS552
D	LYS52
D	LYS318
D	LYS365
D	LYS376
D	LYS462
D	LYS531
D	LYS552
A	LYS365
A	LYS376
A	LYS462
A	LYS531
A	LYS552
B	LYS52
B	LYS318

site_id	SWS_FT_FI8
Number of Residues	24
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:Q8CHT0

Chain	Residue	Details
A	LYS93
B	LYS130
B	LYS175
B	LYS509
C	LYS93
C	LYS99
C	LYS114
C	LYS130
C	LYS175
C	LYS509
D	LYS93
A	LYS99
D	LYS99
D	LYS114
D	LYS130
D	LYS175
D	LYS509
A	LYS114
A	LYS130
A	LYS175
A	LYS509
B	LYS93
B	LYS99
B	LYS114

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)