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Crystal structure of antigen 85C and glycerol

Analyse Crystal structure of antigen 85C and glycerol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HRH
Type: protein
Length: 553 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Antigen 85-C
EC: 2.3.1.-
UniProt: P0A4V4
Pockets: 4 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Antigen 85-C (EC 2.3.1.-)	protein	276	38% helix, 16% strand	P0A4V4
B	Antigen 85-C (EC 2.3.1.-)	protein	277	39% helix, 17% strand	P0A4V4

Ligands and binding sites

GOL · Glycerol · additive · 20 copies · chains A, B

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

Pockets

4 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	743	0.80	0.83	67	GOL
2	58	0.37	0.79	16	empty
3	93	0.33	0.74	21	GOL
4	55	0.31	0.76	16	GOL

Interfaces

1 interface between chains.

A–B · 892 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

3HRH · Crystal Structure of Antigen 85C and Glycerol · 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 P0A4V4
Elsewhere: RCSB PDB 3HRH · PDBe 3HRH · UniProt P0A4V4

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