8RKR

Structure of human DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE (ALDH4A1) complexed with a monophosphate-tweezer

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003842	molecular_function	1-pyrroline-5-carboxylate 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	proline catabolic process
A	0009055	molecular_function	electron transfer activity
A	0010133	biological_process	proline catabolic process to glutamate
A	0016491	molecular_function	oxidoreductase activity
A	0019470	biological_process	4-hydroxyproline catabolic process
A	0042802	molecular_function	identical protein binding
B	0003842	molecular_function	1-pyrroline-5-carboxylate 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	proline catabolic process
B	0009055	molecular_function	electron transfer activity
B	0010133	biological_process	proline catabolic process to glutamate
B	0016491	molecular_function	oxidoreductase activity
B	0019470	biological_process	4-hydroxyproline catabolic process
B	0042802	molecular_function	identical protein binding

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE341-SER352

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

Chain	Residue	Details
A	GLY313-PHE320

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008

Chain	Residue	Details
A	GLU314
B	GLU314

---

site_id	SWS_FT_FI2
Number of Residues	2
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

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000250

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

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000250

Chain	Residue	Details
A	ASN211
B	ASN211

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8CHT0

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

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER44
B	SER44

---

site_id	SWS_FT_FI7
Number of Residues	14
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8CHT0

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

---

site_id	SWS_FT_FI8
Number of Residues	12
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q8CHT0

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

---