Structure of PDB 2ejl Chain A

Receptor sequence

>2ejlA (length=516) Species: 300852 (Thermus thermophilus HB8)

MTVEPFRNEPIETFQTEEARRAMREALRRVREEFGRHYPLYIGGEWVDTK
ERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSR
LLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAAL
RYRYPAVEVVPYPGEDNESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAV
GNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEH
PRIRFINFTGSLEVGLKIYEAAGRLAPGQTWFKRAYVETGGKDAIIVDET
ADFDLAAEGVVVSAYGFQGQKCSAASRLILTQGAYEPVLERVLKRAERLS
VGPAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEGEGYFIA
PTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVY
SRKREHLEWARREFHVGNLYFNRKITGALVGVQPFGGFKLSGTNAKTGAL
DYLRLFLEMKAVAERF

3D structure

• PDB: 2ejl Crystal structure analysis of delta1-pyrroline-5-carboxylate dehydrogenase in ternary complex with inhibitor and NAD
• Chain: A
• Resolution: 1.5 Å

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	SER	A	F185 C322 S323 T476 G477 A478 F485	F185 C322 S323 T476 G477 A478 F485

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

External links

• PDB: RCSB:2ejl, PDBe:2ejl, PDBj:2ejl
• PDBsum: 2ejl
• UniProt: Q5SI02