Structure of PDB 5bsh Chain I Binding Site BS01

Receptor Information
>5bsh Chain I (length=270) Species: 3880 (Medicago truncatula) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKTAIHSNPARRTAF
ESIGITVLSSNDDVVRDSNVVVFSVKPQLLKDVVLKLKPLLTKDKLLVSV
AAGIKMKDLQEWAGHERFIRVMPNTAATVGEAASVMSLGGAATEEDANLI
SQLFGSIGKIWKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGLPR
DLALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGTTIAGVHELEKAG
FRGILMNAVVAAAKRSQELS
Ligand information
Ligand IDPRO
InChIInChI=1S/C5H9NO2/c7-5(8)4-2-1-3-6-4/h4,6H,1-3H2,(H,7,8)/t4-/m0/s1
InChIKeyONIBWKKTOPOVIA-BYPYZUCNSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1C[C@H](NC1)C(=O)O
CACTVS 3.341OC(=O)[C@@H]1CCCN1
CACTVS 3.341OC(=O)[CH]1CCCN1
OpenEye OEToolkits 1.5.0C1CC(NC1)C(=O)O
ACDLabs 10.04O=C(O)C1NCCC1
FormulaC5 H9 N O2
NamePROLINE
ChEMBLCHEMBL54922
DrugBankDB00172
ZINCZINC000000895360
PDB chain5bsh Chain I Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5bsh The structure of Medicago truncatula delta (1)-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants.
Resolution2.1 Å
Binding residue
(original residue number in PDB)
S238 T242 T243
Binding residue
(residue number reindexed from 1)
S234 T238 T239
Annotation score5
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:5bsh, PDBe:5bsh, PDBj:5bsh
PDBsum5bsh
PubMed26579138
UniProtG7KRM5

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