MolNFT v1 · #102953 · protein

The structure of escherichia COLI zapa

4P1M · Cell division protein zapa: “The structure of escherichia COLI zapa”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.44). MolNFT v1 #102953 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4P1M
Type: protein
Length: 213 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein zapa
UniProt: Q1JQN5
Ligands: CL
Pockets: 2 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein zapa	protein	106	73% helix, 11% strand	Q1JQN5
B	Cell division protein zapa	protein	107	69% helix, 13% strand	Q1JQN5

Ligands and binding sites

CL · Chloride ion · ion · chains B

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

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	115	0.44	0.77	21	empty
2	102	0.42	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 1810 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

4P1M · The structure of Escherichia coli ZapA · the same entry in another collection · chain A against A, TM-score 1.00
Q1JQN5 · AlphaFold monomer V2.0 prediction for cell division protein zapa (Q1JQN5) · a predicted model of the same protein · chain B against A, TM-score 0.90

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 Q1JQN5
Elsewhere: RCSB PDB 4P1M · PDBe 4P1M · UniProt Q1JQN5

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