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Hemerythrin-like domain of dcrh I119H mutant (met)

Analyse Hemerythrin-like domain of dcrh I119H mutant (met) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WHN
Type: protein
Length: 266 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemerythrin-like domain protein dcrh
UniProt: Q9REU3
Ligands: CFO, CA
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hemerythrin-like domain protein dcrh	protein	133	82% helix, 0% strand	Q9REU3

Ligands and binding sites

CFO · Chloro diiron-oxo moiety · ligand · 2 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

2 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	312	0.64	0.80	29	empty
2	88	0.34	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 157 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3WHN · Hemerythrin-like domain of DcrH I119H mutant (met) · 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 Q9REU3
Elsewhere: RCSB PDB 3WHN · PDBe 3WHN · UniProt Q9REU3

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