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Internalin domain of listeria monocytogenes inlb: rhombohedral crystal form

Analyse Internalin domain of listeria monocytogenes inlb: rhombohedral crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WQV
Type: protein
Length: 564 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Internalin B
UniProt: P25147
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Internalin B	protein	280	17% helix, 28% strand	P25147
B	Internalin B	protein	284	17% helix, 27% strand	P25147

Ligands and binding sites

PGE · Triethylene glycol · additive · 4 copies · chains A, B
PG4 · Tetraethylene glycol · additive · 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	462	0.68	0.80	58	PGE
2	83	0.46	0.82	20	empty

Interfaces

1 interface between chains.

A–B · 925 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

2WQV · Internalin domain of Listeria monocytogenes InlB: rhombohedral crystal form · 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 P25147
Elsewhere: RCSB PDB 2WQV · PDBe 2WQV · UniProt P25147

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