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Crystal structure of limiting CO2-inducible protein lcib

Analyse Crystal structure of limiting CO2-inducible protein lcib in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5K5W
Type: protein
Length: 424 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Limiting CO2-inducible protein lcib
UniProt: Q0ZAI6
Ligands: ZN
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Limiting CO2-inducible protein lcib	protein	198	43% helix, 22% strand	Q0ZAI6
B	Limiting CO2-inducible protein lcib	protein	226	42% helix, 23% strand	Q0ZAI6

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	453	0.69	0.80	57	ZN
2	50	0.61	0.93	15	empty
3	93	0.43	0.78	21	empty
4	72	0.36	0.77	13	empty

Interfaces

1 interface between chains.

A–B · 1157 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

5K5W · Crystal structure of limiting CO2-inducible protein LCIB · 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 Q0ZAI6
Elsewhere: RCSB PDB 5K5W · PDBe 5K5W · UniProt Q0ZAI6

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