MolNFT v1 · #11997 · protein

Type III secretion chaperone cest

1K3E: “Type III secretion chaperone cest”. X-ray diffraction, 2 pockets (best druggability 0.42). MolNFT v1 #11997 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1K3E
Type: protein
Length: 285 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cest
UniProt: Q47015
Pockets: 2 · best druggability 0.42

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cest	protein	141	37% helix, 26% strand	Q47015
B	Cest	protein	144	35% helix, 27% strand	Q47015

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	65	0.42	0.81	16	empty
2	124	0.37	0.73	26	empty

Interfaces

1 interface between chains.

A–B · 1228 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

1K3E · Type III secretion chaperone CesT · the same entry in another collection · chain A against A, TM-score 1.00
Q47015 · AlphaFold monomer V2.0 prediction for tir chaperone (Q47015) · a predicted model of the same protein · chain B against A, TM-score 0.69

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 Q47015
Elsewhere: RCSB PDB 1K3E · PDBe 1K3E · UniProt Q47015

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