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Crystal structure of the stiv mcp

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

PDB: 2BBD
Type: protein
Length: 1,292 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Coat protein
UniProt: Q6Q0J0
Pockets: 8 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Coat protein	protein	323	13% helix, 49% strand	Q6Q0J0

Ligands and binding sites

MPD · (4S)-2-methyl-2,4-pentanediol · additive · 17 copies · chains A, D, B, C

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

Pockets

8 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	946	0.72	0.76	85	MPD
2	154	0.49	0.78	27	MPD
3	124	0.48	0.79	20	empty
4	78	0.35	0.76	17	MPD
5	79	0.29	0.72	18	empty

Interfaces

1 interface between chains.

A–D · 652 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

2BBD · Crystal Structure of the STIV MCP · 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 Q6Q0J0
Elsewhere: RCSB PDB 2BBD · PDBe 2BBD · UniProt Q6Q0J0

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