MolNFT v1 · #12010 · protein

Type III secretion chaperone sige

1K3S: “Type III secretion chaperone sige”. X-ray diffraction, 1 ligand (PO4), 2 pockets (best druggability 0.63). MolNFT v1 #12010 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1K3S
Type: protein
Length: 215 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sige
UniProt: O30917
Ligands: PO4
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sige	protein	109	39% helix, 30% strand	O30917
B	Sige	protein	106	38% helix, 30% strand	O30917

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A, 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	381	0.63	0.78	30	empty
2	50	0.28	0.75	10	empty

Interfaces

1 interface between chains.

A–B · 1157 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

1K3S · Type III Secretion Chaperone SigE · the same entry in another collection · chain A against A, TM-score 1.00
O30917 · AlphaFold monomer V2.0 prediction for chaperone protein sige (O30917) · a predicted model of the same protein · chain B against A, TM-score 0.94

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 O30917
Elsewhere: RCSB PDB 1K3S · PDBe 1K3S · UniProt O30917

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