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Crystal structure of CPN60.2 from mycobacterium tuberculosis at 2.8A

Analyse Crystal structure of CPN60.2 from mycobacterium tuberculosis at 2.8A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3RTK
Type: protein
Length: 895 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 60 kda chaperonin 2
UniProt: P0A520
Ligands: MG
Pockets: 12 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	60 kda chaperonin 2	protein	448	50% helix, 16% strand	P0A520
B	60 kda chaperonin 2	protein	447	52% helix, 16% strand	P0A520

Ligands and binding sites

MG · Magnesium ion · metal · chains A

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

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	517	0.67	0.78	61	empty
2	279	0.56	0.77	33	empty
3	197	0.55	0.79	27	MG
4	205	0.51	0.76	25	empty
5	192	0.46	0.74	33	empty

Interfaces

1 interface between chains.

A–B · 646 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

3RTK · Crystal structure of Cpn60.2 from Mycobacterium tuberculosis at 2.8A · 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 P0A520
Elsewhere: RCSB PDB 3RTK · PDBe 3RTK · UniProt P0A520

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