Structure of PDB 2bjk Chain A

Receptor sequence
>2bjkA (length=516) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
MTVEPFRNEPIETFQTEEARRAMREALRRVREEFGRHYPLYIGGEWVDTK
ERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSR
LLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAAL
RYRYPAVEVVPYPGEDNESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAV
GNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEH
PRIRFINFTGSLEVGLKIYEAAGRLAPGQTWFKRAYVETGGKDAIIVDET
ADFDLAAEGVVVSAYGFQGQKCSAASRLILTQGAYEPVLERVLKRAERLS
VGPAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEGEGYFIA
PTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVY
SRKREHLEWARREFHVGNLYFNRKITGALVGVQPFGGFKLSGTNAKTGAL
DYLRLFLEMKAVAERF
3D structure
PDB2bjk Crystal Structure of Thermus Thermophilus Delta(1)- Pyrroline-5-Carboxylate Dehydrogenase.
ChainA
Resolution1.4 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 NAD A I180 A181 P182 W183 N184 I189 K207 E210 G240 E241 F258 T259 G260 S261 V264 E288 T289 C322 E417 F419 I180 A181 P182 W183 N184 I189 K207 E210 G240 E241 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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Cellular Component
External links
PDB RCSB:2bjk, PDBe:2bjk, PDBj:2bjk
PDBsum2bjk
PubMed16934832
UniProtQ5SI02

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