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Native aplysia ADP ribosyl cyclase

Analyse Native aplysia ADP ribosyl cyclase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1R12
Type: protein
Length: 502 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADP-ribosyl cyclase
EC: 3.2.2.5
UniProt: P29241
Pockets: 5 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	ADP-ribosyl cyclase (EC 3.2.2.5)	protein	251	43% helix, 13% strand	P29241

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	827	0.75	0.80	67	empty
2	283	0.61	0.79	43	empty
3	255	0.60	0.79	38	empty
4	53	0.33	0.77	12	empty
5	66	0.28	0.73	12	empty

Interfaces

1 interface between chains.

A–B · 1478 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

1R12 · Native Aplysia ADP ribosyl cyclase · the same entry in another collection · chain A against A, TM-score 1.00
P29241 · AlphaFold monomer V2.0 prediction for ADP-ribosyl CYCLASE/CYCLIC ADP- ribose hydrolase… · 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 P29241
Elsewhere: RCSB PDB 1R12 · PDBe 1R12 · UniProt P29241

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