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Improved coordinates for escherichia COLI O157:H7 heme degrading enzyme chus.

Analyse Improved coordinates for escherichia COLI O157:H7 heme degrading enzyme chus. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4CDP
Type: protein
Length: 333 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative HEME/HEMOGLOBIN transport protein
UniProt: Q8X5N8
Ligands: HEM
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative HEME/HEMOGLOBIN transport protein	protein	333	31% helix, 32% strand	Q8X5N8

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
EDO · 1,2-ethanediol · additive · 12 copies · chains A
FMT · Formic acid · additive · chains 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	717	0.70	0.77	66	FMT, HEM
2	374	0.59	0.76	43	EDO

Compared structures

4CDP · Improved coordinates for Escherichia coli O157:H7 heme degrading enzyme ChuS. · 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 Q8X5N8
Elsewhere: RCSB PDB 4CDP · PDBe 4CDP · UniProt Q8X5N8

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