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C-terminal domain of cyclase associated protein with pro 505 replaced by ser (P505S)

Analyse C-terminal domain of cyclase associated protein with pro 505 replaced by ser… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KQ5
Type: protein
Length: 312 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenylyl cyclase-associated protein
UniProt: P17555
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 62% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Adenylyl cyclase-associated protein	protein	156	2% helix, 62% strand	P17555

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	805	0.76	0.80	63	empty

Interfaces

1 interface between chains.

A–B · 514 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

1KQ5 · C-terminal Domain of Cyclase Associated Protein with PRO 505 Replaced by SER (P505S) · the same entry in another collection · chain A against A, TM-score 1.00
P17555 · AlphaFold monomer V2.0 prediction for adenylyl cyclase-associated protein (P17555) · a predicted model of the same protein · chain B against A, TM-score 0.89

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 P17555
Elsewhere: RCSB PDB 1KQ5 · PDBe 1KQ5 · UniProt P17555

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