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Adenylyl cyclase class IV from yersinia pestis

Analyse Adenylyl cyclase class IV from yersinia pestis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FJT
Type: protein
Length: 353 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenylyl cyclase class IV
EC: 4.6.1.1
UniProt: Q7CH76
Ligands: SO4
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenylyl cyclase class IV (EC 4.6.1.1)	protein	178	26% helix, 44% strand	Q7CH76
B	Adenylyl cyclase class IV (EC 4.6.1.1)	protein	175	25% helix, 45% strand	Q7CH76

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	426	0.77	0.86	46	SO4
2	587	0.75	0.82	56	SO4

Interfaces

1 interface between chains.

A–B · 1109 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

2FJT · Adenylyl cyclase class iv from Yersinia pestis · 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 Q7CH76
Elsewhere: RCSB PDB 2FJT · PDBe 2FJT · UniProt Q7CH76

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