MolNFT v1 · #94032 · protein

Structure of the HCP1 protein from E. COLI eaec 042 pathovar, mutants N93W-S158W

4HKH · Putative type VI secretion protein: “Structure of the HCP1 protein from E. COLI eaec 042 pathovar, mutants N93W-S158W”. X-ray diffraction, 1 ligand (SO4), 9 pockets (best druggability 0.43). MolNFT v1 #94032 on GenesisL1: 3D…

PDB: 4HKH
Type: protein
Length: 851 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative type VI secretion protein
UniProt: D3GUW0
Ligands: SO4
Pockets: 9 · best druggability 0.43

Structure

x-ray diffraction · 6 distinct chains · 7% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative type VI secretion protein	protein	149	9% helix, 52% strand	D3GUW0
B	Putative type VI secretion protein	protein	139	7% helix, 53% strand	D3GUW0
D	Putative type VI secretion protein	protein	142	7% helix, 54% strand	D3GUW0
E	Putative type VI secretion protein	protein	137	7% helix, 53% strand	D3GUW0
F	Putative type VI secretion protein	protein	142	7% helix, 53% strand	D3GUW0
G	Putative type VI secretion protein	protein	142	7% helix, 53% strand	D3GUW0

Ligands and binding sites

SO4 · Sulfate ion · ion · 11 copies · chains A, B, D, E, G

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

Pockets

9 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	107	0.43	0.77	21	empty
2	101	0.37	0.75	17	empty
3	83	0.37	0.76	17	empty
4	70	0.35	0.76	18	empty
5	72	0.35	0.76	17	empty

Interfaces

6 interfaces between chains.

A–B · 1195 Å² buried · 15 hydrogen bonds · protein-protein
A–G · 1194 Å² buried · 17 hydrogen bonds · protein-protein
E–F · 1183 Å² buried · 17 hydrogen bonds · protein-protein
F–G · 1183 Å² buried · 16 hydrogen bonds · protein-protein
B–D · 1153 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

4HKH · Structure of the Hcp1 protein from E. coli EAEC 042 pathovar, mutants N93W-S158W · 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 D3GUW0
Elsewhere: RCSB PDB 4HKH · PDBe 4HKH · UniProt D3GUW0

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