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The crystal structure of the bacterial cell division protein zapa

Analyse The crystal structure of the bacterial cell division protein zapa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1W2E
Type: protein
Length: 182 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Zapa
UniProt: Q9HTW3
Pockets: 2 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 74% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Zapa	protein	91	71% helix, 13% strand	Q9HTW3
B	Zapa	protein	91	76% helix, 9% strand	Q9HTW3

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	118	0.40	0.75	15	empty
2	94	0.35	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 1599 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

1W2E · The Crystal Structure of the Bacterial Cell Division Protein ZapA · the same entry in another collection · chain A against A, TM-score 1.00
Q9HTW3 · AlphaFold monomer V2.0 prediction for cell division protein zapa (Q9HTW3) · a predicted model of the same protein · chain A against A, TM-score 0.77

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 Q9HTW3
Elsewhere: RCSB PDB 1W2E · PDBe 1W2E · UniProt Q9HTW3

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