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Structure analysis of adenylate cyclases from trypanosoma brucei in their monomeric state

Analyse Structure analysis of adenylate cyclases from trypanosoma brucei in their… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FX4
Type: protein
Length: 231 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Receptor-type adenylate cyclase gresag 4.3
EC: 4.6.1.1
UniProt: Q99280
Ligands: MG
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Receptor-type adenylate cyclase gresag 4.3 (EC 4.6.1.1)	protein	231	37% helix, 23% strand	Q99280

Ligands and binding sites

MG · Magnesium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	92	0.50	0.82	18	empty

Compared structures

1FX4 · Structure analysis of adenylate cyclases from trypanosoma brucei in their monomeric state · the same entry in another collection · chain A against A, TM-score 1.00
Q99280 · AlphaFold monomer V2.0 prediction for receptor-type adenylate cyclase gresag 4.3 (Q99280) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q99280
Elsewhere: RCSB PDB 1FX4 · PDBe 1FX4 · UniProt Q99280

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