Structure of PDB 5bsg Chain G Binding Site BS02
Receptor Information
>5bsg Chain G (length=269) Species:
3880
(Medicago truncatula) [
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IPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKTAIHSNPARRTAFE
SIGITVLSSNDDVVRDSNVVVFSVKPQLLKDVVLKLKPLLTKDKLLVSVA
AGIKMKDLQEWAGHERFIRVMPNTAATVGEAASVMSLGGAATEEDANLIS
QLFGSIGKIWKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGLPRD
LALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGTTIAGVHELEKAGF
RGILMNAVVAAAKRSQELS
Ligand information
Ligand ID
CL
InChI
InChI=1S/ClH/h1H/p-1
InChIKey
VEXZGXHMUGYJMC-UHFFFAOYSA-M
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Cl-]
Formula
Cl
Name
CHLORIDE ION
ChEMBL
DrugBank
DB14547
ZINC
PDB chain
5bsg Chain G Residue 303 [
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Receptor-Ligand Complex Structure
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PDB
5bsg
The structure of Medicago truncatula delta (1)-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants.
Resolution
1.95 Å
Binding residue
(original residue number in PDB)
S238 T243
Binding residue
(residue number reindexed from 1)
S233 T238
Annotation score
1
Enzymatic activity
Enzyme Commision number
1.5.1.2
: pyrroline-5-carboxylate reductase.
Gene Ontology
Molecular Function
GO:0000166
nucleotide binding
GO:0004735
pyrroline-5-carboxylate reductase activity
GO:0016491
oxidoreductase activity
Biological Process
GO:0006561
proline biosynthetic process
GO:0055129
L-proline biosynthetic process
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:5bsg
,
PDBe:5bsg
,
PDBj:5bsg
PDBsum
5bsg
PubMed
26579138
UniProt
G7KRM5
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