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Crystal structure of triple mutant (kda to egy) of an adenylyl cyclase MA1120 from mycobacterium avium in complex with ATP and calcium ion

Analyse Crystal structure of triple mutant (kda to egy) of an adenylyl cyclase MA1120… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5D0H
Type: protein
Length: 323 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclase
UniProt: V7LAR8
Ligands: ATP, CA
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyclase	protein	162	40% helix, 30% strand	V7LAR8
B	Cyclase	protein	161	42% helix, 27% strand	V7LAR8

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B

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	873	0.79	0.82	67	ATP, CA

Interfaces

1 interface between chains.

A–B · 912 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

5D0H · Crystal Structure of triple mutant (KDA to EGY) of an adenylyl cyclase Ma1120 from… · 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 V7LAR8
Elsewhere: RCSB PDB 5D0H · PDBe 5D0H · UniProt V7LAR8

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