Structure of PDB 2j40 Chain A

Receptor sequence

>2j40A (length=516) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]

MTVEPFRNEPIETFQTEEARRAMREALRRVREEFGRHYPLYIGGEWVDTK
ERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSR
LLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAAL
RYRYPAVEVVPYPGEDNESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAV
GNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEH
PRIRFINFTGSLEVGLKIYEAAGRLAPGQTWFKRAYVETGGKDAIIVDET
ADFDLAAEGVVVSAYGFQGQKCSAASRLILTQGAYEPVLERVLKRAERLS
VGPAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEGEGYFIA
PTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVY
SRKREHLEWARREFHVGNLYFNRKITGALVGVQPFGGFKLSGTNAKTGAL
DYLRLFLEMKAVAERF

3D structure

PDB

2j40 Crystal Structure of Ternary Complex of Delta1-Pyrroline-5-Carboxylate Dehydrogenase with Substrate Mimic and Co-Factoer

Chain

Resolution

2.1 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	N184 K207 E288 C322 E417 T497
Catalytic site (residue number reindexed from 1)	N184 K207 E288 C322 E417 T497
Enzyme Commision number	1.2.1.88: L-glutamate gamma-semialdehyde dehydrogenase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	PRO	A	E137 F185 C322 S323 G477 A478 F485	E137 F185 C322 S323 G477 A478 F485
BS02	NAD	A	I180 A181 P182 W183 N184 I189 K207 E210 G240 E241 A245 F258 T259 G260 S261 V264 E288 T289 C322 E417 F419	I180 A181 P182 W183 N184 I189 K207 E210 G240 E241 A245 F258 T259 G260 S261 V264 E288 T289 C322 E417 F419

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0003842	1-pyrroline-5-carboxylate dehydrogenase activity
GO:0016491	oxidoreductase activity
GO:0016620	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

	Biological Process
GO:0010133	proline catabolic process to glutamate

	Cellular Component
GO:0009898	cytoplasmic side of plasma membrane

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:2j40, PDBe:2j40, PDBj:2j40
PDBsum	2j40
PubMed
UniProt	Q5SI02

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