Structure of PDB 5bse Chain G Binding Site BS01

Receptor Information
>5bse Chain G (length=268) Species: 3880 (Medicago truncatula) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKTAIHSNPARRTAFES
IGITVLSSNDDVVRDSNVVVFSVKPQLLKDVVLKLKPLLTKDKLLVSVAA
GIKMKDLQEWAGHERFIRVMPNTAATVGEAASVMSLGGAATEEDANLISQ
LFGSIGKIWKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGLPRDL
ALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGTTIAGVHELEKAGFR
GILMNAVVAAAKRSQELS
Ligand information
Ligand IDCL
InChIInChI=1S/ClH/h1H/p-1
InChIKeyVEXZGXHMUGYJMC-UHFFFAOYSA-M
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Cl-]
FormulaCl
NameCHLORIDE ION
ChEMBL
DrugBankDB14547
ZINC
PDB chain5bse Chain G Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5bse The structure of Medicago truncatula delta (1)-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		S238 T242 T243
Binding residue
(residue number reindexed from 1)		S232 T236 T237
Annotation score1
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5bse, PDBe:5bse, PDBj:5bse
PDBsum5bse
PubMed26579138
UniProtG7KRM5

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