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Crystal structure of branched-chain amino acid aminotransferase from thermobaculum terrenum in pmp-form

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

PDB: 6Q8E
Type: protein
Length: 307 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Branched-chain-amino-acid aminotransferase
EC: 2.6.1.42
UniProt: D1CCW1
Ligands: PMP, CL
Pockets: 3 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Branched-chain-amino-acid aminotransferase (EC 2.6.1.42)	protein	307	31% helix, 30% strand	D1CCW1

Ligands and binding sites

PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · chains A
CL · Chloride ion · ion · 5 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	219	0.58	0.80	40	PMP, CL
2	121	0.42	0.75	16	empty
3	64	0.33	0.76	13	empty

Compared structures

6Q8E · Crystal structure of branched-chain amino acid aminotransferase from Thermobaculum… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt D1CCW1
Elsewhere: RCSB PDB 6Q8E · PDBe 6Q8E · UniProt D1CCW1

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