Research workbench

Alanine racemase from bacillus anthracis (ames)

Analyse Alanine racemase from bacillus anthracis (ames) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HA1
Type: protein
Length: 772 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alanine racemase
EC: 5.1.1.1
UniProt: Q81VF6
Ligands: CL
Pockets: 13 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Alanine racemase (EC 5.1.1.1)	protein	386	32% helix, 27% strand	Q81VF6

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A, B
ACT · Acetate ion · additive · 2 copies · chains A, B

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

Pockets

13 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	66	0.74	0.99	27	empty
2	140	0.62	0.86	33	ACT
3	133	0.62	0.86	32	ACT
4	100	0.57	0.85	21	empty
5	86	0.54	0.85	18	empty

Interfaces

1 interface between chains.

A–B · 3708 Å² buried · 57 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (cofactor).

Compared structures

3HA1 · Alanine racemase from Bacillus Anthracis (Ames) · 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 Q81VF6
Elsewhere: RCSB PDB 3HA1 · PDBe 3HA1 · UniProt Q81VF6

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