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Crystal structure of the fha domain of CT664 protein from chlamydia trachomatis

Analyse Crystal structure of the fha domain of CT664 protein from chlamydia trachomatis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GQS
Type: protein
Length: 201 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenylate cyclase-like protein
UniProt: O84671
Ligands: PO4
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenylate cyclase-like protein	protein	100	0% helix, 45% strand	O84671
B	Adenylate cyclase-like protein	protein	101	0% helix, 46% strand	O84671

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	59	0.38	0.79	15	empty

Interfaces

1 interface between chains.

A–B · 572 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3GQS · Crystal structure of the FHA domain of CT664 protein from Chlamydia trachomatis · the same entry in another collection · chain A against A, TM-score 1.00

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 O84671
Elsewhere: RCSB PDB 3GQS · PDBe 3GQS · UniProt O84671

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