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Crystal structure of the human C-terminal CAP1-adenylyl cyclase associated protein

Analyse Crystal structure of the human C-terminal CAP1-adenylyl cyclase associated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1K8F
Type: protein
Length: 628 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenylyl cyclase-associated protein
UniProt: Q01518
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 62% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Adenylyl cyclase-associated protein	protein	157	0% helix, 62% strand	Q01518

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	430	0.56	0.74	44	empty

Interfaces

4 interfaces between chains.

A–B · 1249 Å² buried · 13 hydrogen bonds · protein-protein
C–D · 1247 Å² buried · 13 hydrogen bonds · protein-protein
A–D · 95 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 35 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1K8F · Crystal structure of the human C-terminal CAP1-adenylyl cyclase associated protein · the same entry in another collection · chain D against D, TM-score 1.00
Q01518 · AlphaFold monomer V2.0 prediction for adenylyl cyclase-associated protein 1 (Q01518) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q01518
Elsewhere: RCSB PDB 1K8F · PDBe 1K8F · UniProt Q01518

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