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Crystal structure of a bacterial bestrophin homolog from klebsiella pneumoniae with a mutation I180A

Analyse Crystal structure of a bacterial bestrophin homolog from klebsiella pneumoniae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IV0
Type: protein
Length: 1,345 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bestrophin homolog
UniProt: W1ELP7
Ligands: ZN
Pockets: 16 · best druggability 0.83

Structure

x-ray diffraction · 4 distinct chains · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Bestrophin homolog	protein	268	77% helix, 1% strand	W1ELP7
B	Bestrophin homolog	protein	270	77% helix, 0% strand	W1ELP7
C	Bestrophin homolog	protein	269	80% helix, 0% strand	W1ELP7
E	Bestrophin homolog	protein	270	79% helix, 0% strand	W1ELP7

Ligands and binding sites

ZN · Zinc ion · metal · 15 copies · chains A, E, B, C, D

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

Pockets

16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	709	0.83	0.86	102	empty
2	128	0.74	0.93	28	empty
3	228	0.68	0.85	42	empty
4	669	0.65	0.75	45	empty
5	271	0.64	0.81	49	empty

Interfaces

5 interfaces between chains.

A–B · 2668 Å² buried · 29 hydrogen bonds · protein-protein
C–D · 2573 Å² buried · 25 hydrogen bonds · protein-protein
A–E · 2477 Å² buried · 20 hydrogen bonds · protein-protein
C–E · 2475 Å² buried · 19 hydrogen bonds · protein-protein
B–D · 2453 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

6IV0 · Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae with a… · 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 W1ELP7
Elsewhere: RCSB PDB 6IV0 · PDBe 6IV0 · UniProt W1ELP7

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