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Crystal structure of conserved domain protein from vibrio cholerae O1 biovar eltor str. N16961

Analyse Crystal structure of conserved domain protein from vibrio cholerae O1 biovar… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LKV
Type: protein
Length: 296 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized conserved domain protein
UniProt: Q9KT04
Ligands: PHE, ZN, SO4
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized conserved domain protein	protein	296	43% helix, 21% strand	Q9KT04

Ligands and binding sites

PHE · Phenylalanine · ligand · chains A
ZN · Zinc ion · metal · 3 copies · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.35	0.77	17	empty

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

3LKV · Crystal structure of conserved domain protein from vibrio cholerae o1 biovar eltor str.… · 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 Q9KT04
Elsewhere: RCSB PDB 3LKV · PDBe 3LKV · UniProt Q9KT04

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