Structure of PDB 5uau Chain D

Receptor sequence
>5uauD (length=275) Species: 9606 (Homo sapiens) [Search protein sequence]
MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGV
KLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVT
ISSIEKKLSAFRPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLME
QLLSSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRR
LAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGF
RSLLINAVEASCIRTRELQSMADQE
3D structure
PDB5uau Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.
ChainD
Resolution1.9 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 D T171 G175 T171 G175
BS02 PRO D G236 A237 T238 G236 A237 T238
BS03 PRO D T137 E163 E164 T137 E163 E164
Gene Ontology
Molecular Function
GO:0004735 pyrroline-5-carboxylate reductase activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
Biological Process
GO:0006561 proline biosynthetic process
GO:0034599 cellular response to oxidative stress
GO:0051881 regulation of mitochondrial membrane potential
GO:0055129 L-proline biosynthetic process
GO:1903377 negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5uau, PDBe:5uau, PDBj:5uau
PDBsum5uau
PubMed28258219
UniProtP32322|P5CR1_HUMAN Pyrroline-5-carboxylate reductase 1, mitochondrial (Gene Name=PYCR1)

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