Structure of PDB 2izz Chain C

Receptor sequence
>2izzC (length=276) Species: 9606 (Homo sapiens) [Search protein sequence]
SMSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMG
VKLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGV
TISSIEKKLSAFRPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLM
EQLLSSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPR
RLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGG
FRSLLINAVEASCIRTRELQSMADQE
3D structure
PDB2izz Crystal Structure of Human Pyrroline-5-Carboxylate Reductase
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 NAD C G7 A8 G9 Q10 L11 S34 P35 N56 A69 V70 K71 C95 A96 A97 T122 T124 G8 A9 G10 Q11 L12 S35 P36 N57 A70 V71 K72 C96 A97 A98 T123 T125
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:2izz, PDBe:2izz, PDBj:2izz
PDBsum2izz
PubMed
UniProtP32322|P5CR1_HUMAN Pyrroline-5-carboxylate reductase 1, mitochondrial (Gene Name=PYCR1)

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