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Crystal structure of a bacterial bestrophin homolog from klebsiella pneumoniae with a mutation Y211A

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: 6IV2
Type: protein
Length: 1,329 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bestrophin homolog
UniProt: W1ELP7
Ligands: ZN
Pockets: 20 · best druggability 0.78

Structure

x-ray diffraction · 5 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bestrophin homolog	protein	267	79% helix, 0% strand	W1ELP7
B	Bestrophin homolog	protein	267	80% helix, 1% strand	W1ELP7
C	Bestrophin homolog	protein	262	84% helix, 0% strand	W1ELP7
D	Bestrophin homolog	protein	268	81% helix, 1% strand	W1ELP7
E	Bestrophin homolog	protein	265	81% helix, 0% strand	W1ELP7

Ligands and binding sites

ZN · Zinc ion · metal · 12 copies · chains A, E, B, D, C

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

Pockets

20 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	350	0.78	0.88	52	empty
2	224	0.76	0.90	31	empty
3	353	0.73	0.85	45	empty
4	90	0.70	0.93	19	empty
5	650	0.69	0.78	48	empty

Interfaces

9 interfaces between chains.

C–D · 2459 Å² buried · 21 hydrogen bonds · protein-protein
A–E · 2448 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 2435 Å² buried · 23 hydrogen bonds · protein-protein
B–D · 2400 Å² buried · 21 hydrogen bonds · protein-protein
C–E · 2287 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

6IV2 · 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 6IV2 · PDBe 6IV2 · UniProt W1ELP7

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