Structure of PDB 5bsg Chain D

Receptor sequence
>5bsgD (length=271) Species: 3880 (Medicago truncatula) [Search protein sequence]
IPIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKTAIHSNPARRTA
FESIGITVLSSNDDVVRDSNVVVFSVKPQLLKDVVLKLKPLLTKDKLLVS
VAAGIKMKDLQEWAGHERFIRVMPNTAATVGEAASVMSLGGAATEEDANL
ISQLFGSIGKIWKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGLP
RDLALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGTTIAGVHELEKA
GFRGILMNAVVAAAKRSQELS
3D structure
PDB5bsg The structure of Medicago truncatula delta (1)-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants.
ChainD
Resolution1.95 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D G17 G19 K20 M21 H45 S46 N47 N65 S78 V79 K80 V104 A105 A106 G14 G16 K17 M18 H42 S43 N44 N62 S75 V76 K77 V101 A102 A103
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:5bsg, PDBe:5bsg, PDBj:5bsg
PDBsum5bsg
PubMed26579138
UniProtG7KRM5

[Back to BioLiP]