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Crystal structure of a putative C-S lyase from bacillus anthracis

Analyse Crystal structure of a putative C-S lyase from bacillus anthracis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3T32
Type: protein
Length: 720 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminotransferase, class I/II
UniProt: Q81K67
Pockets: 7 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Aminotransferase, class I/II	protein	360	45% helix, 17% strand	Q81K67

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	184	0.82	0.96	24	empty
2	231	0.59	0.80	43	empty
3	297	0.57	0.76	52	empty
4	96	0.37	0.75	27	empty
5	70	0.33	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 1827 Å² buried · 25 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 modified (engineered, cofactor).

Compared structures

3T32 · Crystal structure of a putative C-S lyase from Bacillus anthracis · the same entry in another collection · chain B against B, 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 Q81K67
Elsewhere: RCSB PDB 3T32 · PDBe 3T32 · UniProt Q81K67

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