MolNFT v1 · #65842 · protein

Crystal structure of uncharacterized conserved protein with double- stranded beta-helix domain (YP_001338853.1) from klebsiella pneumoniae subsp. pneumoniae mgh 78578 at 1.80 a resolution

3H8U · Uncharacterized conserved protein with double-stranded…: “Crystal structure of uncharacterized conserved protein with double- stranded beta-helix domain…”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.49).…

PDB: 3H8U
Type: protein
Length: 237 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized conserved protein with double-stranded beta-helix domain
UniProt: A6TJ50
Ligands: SO4
Pockets: 2 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized conserved protein with double-stranded beta-helix domain	protein	122	3% helix, 48% strand	A6TJ50
B	Uncharacterized conserved protein with double-stranded beta-helix domain	protein	115	3% helix, 50% strand	A6TJ50

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B
GOL · Glycerol · additive · chains A, B
2PE · Nonaethylene glycol · additive · chains 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	110	0.49	0.80	20	empty
2	65	0.39	0.79	25	empty

Interfaces

1 interface between chains.

A–B · 1659 Å² buried · 28 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

3H8U · Crystal structure of uncharacterized conserved protein with double-stranded beta-helix… · 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 A6TJ50
Elsewhere: RCSB PDB 3H8U · PDBe 3H8U · UniProt A6TJ50

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