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Crystal structure of eschelichia COLI branched-chain amino acid aminotransferase.

Analyse Crystal structure of eschelichia COLI branched-chain amino acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1I1L
Type
protein
Length
912 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Branched-chain amino acid aminotransferase
EC
2.6.1.42
UniProt
P00510
Ligands
PLP, 2ML
Pockets
10 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CBranched-chain amino acid aminotransferase (EC 2.6.1.42)protein30429% helix, 26% strandP00510

Ligands and binding sites

  • PLP · Pyridoxal-5'-phosphate · ligand · 3 copies · chains A, B, C
  • 2ML · 2-methylleucine · ligand · 3 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110950.840.8499empty
23650.730.8434empty
32260.700.8742PLP, 2ML
42400.700.8642PLP, 2ML
53750.690.8158PLP, 2ML

Interfaces

3 interfaces between chains.

  • B–C · 660 Ų buried · 8 hydrogen bonds · protein-protein
  • A–C · 659 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 657 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 1I1L · Crystal structure of eschelichia COLI branched-chain amino acid aminotransferase. · the same entry in another collection · chain A against A, TM-score 1.00

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