MolNFT v1 · #59401 · protein

Crystal structure of a DUF692 family protein (HS_1138) from haemophilus somnus 129PT at 2.20 a resolution

3BWW · Protein of unknown function DUF692/COG3220: “Crystal structure of a DUF692 family protein (HS_1138) from haemophilus somnus 129PT at 2.20 a resolution”. X-ray diffraction, 1 ligand (FE), 2 pockets (best druggability 0.61). MolNFT v1…

PDB: 3BWW
Type: protein
Length: 253 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein of unknown function DUF692/COG3220
UniProt: Q0I408
Ligands: FE
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein of unknown function DUF692/COG3220	protein	253	47% helix, 13% strand	Q0I408

Ligands and binding sites

FE · Fe (III) ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A
CAC · Cacodylate ion · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	136	0.61	0.85	24	EDO
2	134	0.44	0.76	27	FE, CAC

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

3BWW · Crystal structure of a duf692 family protein (hs_1138) from haemophilus somnus 129pt at… · 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 Q0I408
Elsewhere: RCSB PDB 3BWW · PDBe 3BWW · UniProt Q0I408

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