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Crystal structure of the C-terminal extracellular domain of mycobacterium tuberculosis embc

Analyse Crystal structure of the C-terminal extracellular domain of mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PTY
Type: protein
Length: 284 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arabinosyltransferase C
EC: 2.4.2.-
UniProt: P72059
Ligands: AFO, CA, PO4
Pockets: 2 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Arabinosyltransferase C (EC 2.4.2.-)	protein	284	17% helix, 31% strand	P72059

Ligands and binding sites

AFO · octyl alpha-D-arabinofuranoside · ligand · chains A
CA · Calcium ion · metal · chains A
PO4 · Phosphate ion · ion · chains A

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

Pockets

2 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	204	0.52	0.77	36	empty
2	139	0.40	0.74	23	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3PTY · Crystal structure of the C-terminal extracellular domain of Mycobacterium tuberculosis… · 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 P72059
Elsewhere: RCSB PDB 3PTY · PDBe 3PTY · UniProt P72059

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