MolNFT v1 · #116003 · protein

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

5D0G: “Crystal structure of triple mutant (kda to egy) of adenylyl cyclase MA1120 from mycobacterium avium in…”. X-ray diffraction, 2 ligands (GTP, CA), 2 pockets (best druggability 0.79). MolNFT v1 #116003 on GenesisL1: 3D structure…

PDB: 5D0G
Type: protein
Length: 318 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclase
UniProt: V7LAR8
Ligands: GTP, CA
Pockets: 2 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyclase	protein	162	41% helix, 31% strand	V7LAR8
B	Cyclase	protein	156	40% helix, 32% strand	V7LAR8

Ligands and binding sites

GTP · Guanosine-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

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	689	0.79	0.83	64	GTP, CA
2	59	0.30	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 1054 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

5D0G · Crystal structure of triple mutant (KDA to EGY) of 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 5D0G · PDBe 5D0G · UniProt V7LAR8

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