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Crystal structure of human 1-pyrroline-5-carboxylate dehydrogenase

Analyse Crystal structure of human 1-pyrroline-5-carboxylate dehydrogenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3V9G
Type
protein
Length
2,162 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
EC
1.5.1.12
UniProt
P30038
Pockets
20 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BDelta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (EC 1.5.1.12)protein54141% helix, 23% strandP30038
C, DDelta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (EC 1.5.1.12)protein54041% helix, 23% strandP30038

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11340.790.9730empty
21200.760.9532empty
34930.760.8467empty
44400.760.8561empty
55040.760.8466empty

Interfaces

4 interfaces between chains.

  • A–B · 4535 Ų buried · 75 hydrogen bonds · protein-protein
  • C–D · 4531 Ų buried · 70 hydrogen bonds · protein-protein
  • B–D · 670 Ų buried · 19 hydrogen bonds · protein-protein
  • A–C · 571 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 3V9G · Crystal structure of human 1-pyrroline-5-carboxylate dehydrogenase · the same entry in another collection · chain D against D, TM-score 1.00
  • P30038 · AlphaFold monomer V2.0 prediction for delta-1-pyrroline-5-carboxylate dehydrogenase… · a predicted model of the same protein · chain C against A, TM-score 1.00

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