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Crystal structure of a LIN0012 protein from listeria innocua

Analyse Crystal structure of a LIN0012 protein from listeria innocua in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3K17
Type: protein
Length: 1,420 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: LIN0012 protein
UniProt: Q92FU1
Pockets: 19 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	LIN0012 protein	protein	355	46% helix, 21% strand	Q92FU1

Ligands and binding sites

PGE · Triethylene glycol · additive · chains A, B

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

Pockets

19 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1123	0.83	0.84	99	empty
2	450	0.74	0.84	43	empty
3	457	0.73	0.83	45	empty
4	404	0.69	0.81	29	empty
5	143	0.61	0.84	19	empty

Interfaces

3 interfaces between chains.

A–B · 1127 Å² buried · 11 hydrogen bonds · protein-protein
C–D · 992 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 601 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 modified (engineered).

Compared structures

3K17 · Crystal structure of a Lin0012 protein from Listeria innocua · 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 Q92FU1
Elsewhere: RCSB PDB 3K17 · PDBe 3K17 · UniProt Q92FU1

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