Structure of PDB 4ihi Chain A

Receptor sequence
>4ihiA (length=535) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
MDAITQVPVPANEPVHDYAPKSPERTRLRTELASLADHPIDLPHVIGGRH
RMGDGERIDVVQPHRHAARLGTLTNATHADAAAAVEAAMSAKSDWAALPF
DERAAVFLRAADLLAGPWREKIAAATMLGQSKSVYQAEIDAVCELIDFWR
FNVAFARQILEQQPISGPGEWNRIDYRPLDGFVYAITPFNFTSIAGNLPT
APALMGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSD
VALADPRLAGIHFTGSTATFGHLWQWVGTNIGRYHSYPRLVGETGGKDFV
VAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAK
AAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAVTVAVGGEYD
DSEGYFVRPTVLLSDDPEYFGPLLSVHVYPDERYEQILDVIDTGSRYALT
GAVIADDRQAVLTALDRLRFAAGNFYVNDKPTGAVVGRQPFGGARGSDTN
DKAGSPLNLLRWTSARSIKETFVAATDHIYPHMAV
3D structure
PDB4ihi Characterization of the proline-utilization pathway in Mycobacterium tuberculosis through structural and functional studies.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N190 K212 E293 C327 E425 A510
Catalytic site (residue number reindexed from 1) N190 K212 E293 C327 E418 A503
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 I186 T187 P188 F189 N190 I194 K212 S214 G245 S249 T264 G265 S266 T269 E293 T294 C327 F427 I186 T187 P188 F189 N190 I194 K212 S214 G245 S249 T264 G265 S266 T269 E293 T294 C327 F420
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
GO:0046872 metal ion binding
Biological Process
GO:0006560 proline metabolic 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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Cellular Component
External links
PDB RCSB:4ihi, PDBe:4ihi, PDBj:4ihi
PDBsum4ihi
PubMed24699642
UniProtO50443

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