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Putative adenylyl cyclase HPAC1 from hippeastrum reveals a dominant triphophatase activity

Analyse Putative adenylyl cyclase HPAC1 from hippeastrum reveals a dominant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6YP4
Type: protein
Length: 210 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenylate cyclase
UniProt: E1AQY1
Ligands: GCP, MG, CL
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenylate cyclase	protein	210	32% helix, 42% strand	E1AQY1

Ligands and binding sites

GCP · Phosphomethylphosphonic acid guanylate ester · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
CL · Chloride ion · ion · 3 copies · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A

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	318	0.69	0.83	47	GCP, MG, CL
2	77	0.51	0.84	23	EDO

Compared structures

6YP4 · Putative adenylyl cyclase HpAC1 from Hippeastrum reveals a dominant triphophatase activity · 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 E1AQY1
Elsewhere: RCSB PDB 6YP4 · PDBe 6YP4 · UniProt E1AQY1

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