MolNFT v1 · #115510 · protein

Crystal structure of branched-chain aminotransferase from thermophilic archaea geoglobus acetivorans

5CM0 · Branched-chain transaminase: “Crystal structure of branched-chain aminotransferase from thermophilic archaea geoglobus acetivorans”. X-ray diffraction, 1 ligand (PLP), 8 pockets (best druggability 0.72). MolNFT v1 #115510 on…

PDB: 5CM0
Type: protein
Length: 849 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Branched-chain transaminase
UniProt: A0A0A7GJ30
Ligands: PLP
Pockets: 8 · best druggability 0.72

Structure

x-ray diffraction · 3 distinct chains · 31% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Branched-chain transaminase	protein	282	31% helix, 30% strand	A0A0A7GJ30
B	Branched-chain transaminase	protein	287	30% helix, 28% strand	A0A0A7GJ30
C	Branched-chain transaminase	protein	280	31% helix, 30% strand	A0A0A7GJ30

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · 3 copies · chains A, B, C
GOL · Glycerol · additive · 2 copies · chains A, C

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

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	535	0.72	0.81	65	empty
2	383	0.69	0.82	43	PLP
3	321	0.69	0.83	43	PLP
4	234	0.57	0.79	45	PLP
5	67	0.32	0.75	15	empty

Interfaces

3 interfaces between chains.

A–C · 2445 Å² buried · 28 hydrogen bonds · protein-protein
B–C · 698 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 690 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 cofactor (pyridoxal phosphate Schiff base).

Compared structures

5CM0 · Crystal structure of branched-chain aminotransferase from thermophilic archaea Geoglobus… · 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 A0A0A7GJ30
Elsewhere: RCSB PDB 5CM0 · PDBe 5CM0 · UniProt A0A0A7GJ30

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