Structure of PDB 5bsh Chain I

Receptor sequence
>5bshI (length=270) Species: 3880 (Medicago truncatula) [Search protein sequence]
PIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKTAIHSNPARRTAF
ESIGITVLSSNDDVVRDSNVVVFSVKPQLLKDVVLKLKPLLTKDKLLVSV
AAGIKMKDLQEWAGHERFIRVMPNTAATVGEAASVMSLGGAATEEDANLI
SQLFGSIGKIWKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGLPR
DLALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGTTIAGVHELEKAG
FRGILMNAVVAAAKRSQELS
3D structure
PDB5bsh The structure of Medicago truncatula delta (1)-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants.
ChainI
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.5.1.2: pyrroline-5-carboxylate reductase.
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 PRO I S238 T242 T243 S234 T238 T239
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
View graph for
Biological Process
External links
PDB RCSB:5bsh, PDBe:5bsh, PDBj:5bsh
PDBsum5bsh
PubMed26579138
UniProtG7KRM5

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