3V9I

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

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	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	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	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	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 PROSITE/UniProt

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	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22516612","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	28
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	11
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8CHT0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	23
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8CHT0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	24
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8CHT0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---