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Crystal structure of N-terminal truncated pseudopilin pulg

Analyse Crystal structure of N-terminal truncated pseudopilin pulg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1T92
Type: protein
Length: 216 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: General secretion pathway protein G
UniProt: P15746
Ligands: ZN
Pockets: 2 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	General secretion pathway protein G	protein	108	32% helix, 14% strand	P15746

Ligands and binding sites

ZN · Zinc ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	127	0.45	0.77	21	empty
2	119	0.42	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 1385 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

1T92 · Crystal structure of N-terminal truncated pseudopilin PulG · the same entry in another collection · chain A against A, TM-score 1.00
P15746 · AlphaFold monomer V2.0 prediction for type II secretion system core protein G (P15746) · a predicted model of the same protein · chain A against A, TM-score 0.85

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 P15746
Elsewhere: RCSB PDB 1T92 · PDBe 1T92 · UniProt P15746

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