Structure of PDB 5uau Chain B

Receptor sequence
>5uauB (length=277) Species: 9606 (Homo sapiens) [Search protein sequence]
FQSMSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRK
MGVKLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAA
GVTISSIEKKLSAFRPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGR
LMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGL
PRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLES
GGFRSLLINAVEASCIRTRELQSMADQ
3D structure
PDB5uau Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.
ChainB
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 B T171 G175 T174 G178
BS02 PRO B V231 A237 T238 V234 A240 T241
BS03 PRO B T137 E163 E164 T140 E166 E167
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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