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Crystal structure of HCP1 from salmonella typhimurium

Analyse Crystal structure of HCP1 from salmonella typhimurium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5XHH
Type: protein
Length: 429 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HCP1 family type VI secretion system effector
UniProt: H9L4J2
Pockets: 3 · best druggability 0.81

Structure

x-ray diffraction · 3 distinct chains · 7% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	HCP1 family type VI secretion system effector	protein	150	7% helix, 52% strand	H9L4J2
B	HCP1 family type VI secretion system effector	protein	138	8% helix, 55% strand	H9L4J2
C	HCP1 family type VI secretion system effector	protein	141	8% helix, 53% strand	H9L4J2

Pockets

3 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	1016	0.81	0.82	86	empty
2	132	0.40	0.74	25	empty
3	57	0.31	0.76	17	empty

Interfaces

2 interfaces between chains.

A–C · 1211 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 311 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5XHH · crystal structure of Hcp1 from Salmonella typhimurium · 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 H9L4J2
Elsewhere: RCSB PDB 5XHH · PDBe 5XHH · UniProt H9L4J2

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