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Crystal structure of thermotoga maritima CSM2

Analyse Crystal structure of thermotoga maritima CSM2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5AN6
Type: protein
Length: 369 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CRISPR-associated protein, CSM2 family
UniProt: Q9X2D0
Ligands: CD
Pockets: 2 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 83% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	CRISPR-associated protein, CSM2 family	protein	123	83% helix, 0% strand	Q9X2D0

Ligands and binding sites

CD · Cadmium ion · metal · 7 copies · chains B, C, 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	77	0.34	0.75	21	CD
2	50	0.31	0.77	15	empty

Interfaces

3 interfaces between chains.

B–C · 4350 Å² buried · 45 hydrogen bonds · protein-protein
A–C · 361 Å² buried · 0 hydrogen bonds · protein-protein
A–B · 113 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5AN6 · Crystal structure of Thermotoga maritima Csm2 · 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 Q9X2D0
Elsewhere: RCSB PDB 5AN6 · PDBe 5AN6 · UniProt Q9X2D0

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