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Mycobacterial adenylyl cyclase RV1264, holoenzyme, active state

Analyse Mycobacterial adenylyl cyclase RV1264, holoenzyme, active state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Y11
Type: protein
Length: 364 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein RV1264/MT1302
EC: 4.6.1.1
UniProt: Q11055
Ligands: SO4
Pockets: 3 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein RV1264/MT1302 (EC 4.6.1.1)	protein	364	48% helix, 16% strand	Q11055

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
1PE · Pentaethylene glycol · additive · chains A
GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 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	237	0.50	0.74	27	empty
2	204	0.49	0.75	26	empty
3	232	0.49	0.74	26	1PE

Compared structures

1Y11 · Mycobacterial adenylyl cyclase Rv1264, holoenzyme, active state · 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 Q11055
Elsewhere: RCSB PDB 1Y11 · PDBe 1Y11 · UniProt Q11055

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