Structure of PDB 5bsf Chain D

Receptor sequence
>5bsfD (length=271) Species: 3880 (Medicago truncatula) [Search protein sequence]
IPIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKTAIHSNPARRTA
FESIGITVLSSNDDVVRDSNVVVFSVKPQLLKDVVLKLKPLLTKDKLLVS
VAAGIKMKDLQEWAGHERFIRVMPNTAATVGEAASVMSLGGAATEEDANL
ISQLFGSIGKIWKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGLP
RDLALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGTTIAGVHELEKA
GFRGILMNAVVAAAKRSQELS
3D structure
PDB5bsf The structure of Medicago truncatula delta (1)-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants.
ChainD
Resolution1.85 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 NAD D G17 G19 K20 M21 H45 N65 V79 K80 L83 V104 A105 A106 P127 N128 G14 G16 K17 M18 H42 N62 V76 K77 L80 V101 A102 A103 P124 N125
BS02 CL D S238 T243 S235 T240
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:5bsf, PDBe:5bsf, PDBj:5bsf
PDBsum5bsf
PubMed26579138
UniProtG7KRM5

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