MolNFT v1 · #155254 · protein

Apo-bacf structure from bacillus subtillis

6L1L · Aminotransferase: “Apo-bacf structure from bacillus subtillis”. X-ray diffraction, 1 ligand (PLP), 10 pockets (best druggability 0.83). MolNFT v1 #155254 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6L1L
Type: protein
Length: 768 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminotransferase
EC: 2.6.1.-
UniProt: A0A164UM01
Ligands: PLP
Pockets: 10 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminotransferase (EC 2.6.1.-)	protein	375	43% helix, 15% strand	A0A164UM01
B	Aminotransferase (EC 2.6.1.-)	protein	393	46% helix, 15% strand	A0A164UM01

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	201	0.83	0.97	39	empty
2	271	0.76	0.89	51	PLP
3	232	0.75	0.89	47	PLP
4	224	0.52	0.77	34	empty
5	98	0.51	0.82	23	empty

Interfaces

1 interface between chains.

A–B · 3027 Å² buried · 40 hydrogen bonds · protein-protein

Compared structures

6L1L · Apo-BacF structure from Bacillus subtillis · 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 A0A164UM01
Elsewhere: RCSB PDB 6L1L · PDBe 6L1L · UniProt A0A164UM01

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