Structure of PDB 5bsg Chain C

Receptor sequence
>5bsgC (length=270) Species: 3880 (Medicago truncatula) [Search protein sequence]
PIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKTAIHSNPARRTAF
ESIGITVLSSNDDVVRDSNVVVFSVKPQLLKDVVLKLKPLLTKDKLLVSV
AAGIKMKDLQEWAGHERFIRVMPNTAATVGEAASVMSLGGAATEEDANLI
SQLFGSIGKIWKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGLPR
DLALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGTTIAGVHELEKAG
FRGILMNAVVAAAKRSQELS
3D structure
PDB5bsg The structure of Medicago truncatula delta (1)-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants.
ChainC
Resolution1.95 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 NAP C G17 G19 K20 M21 H45 S46 N47 N65 S78 V79 K80 L83 V104 A105 A106 P127 G13 G15 K16 M17 H41 S42 N43 N61 S74 V75 K76 L79 V100 A101 A102 P123
BS02 CL C S238 T243 S234 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:5bsg, PDBe:5bsg, PDBj:5bsg
PDBsum5bsg
PubMed26579138
UniProtG7KRM5

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