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Crystal structure of mature cpaf

Analyse Crystal structure of mature cpaf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DOR
Type: protein
Length: 1,049 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein CT_858
UniProt: O84866
Ligands: SO4
Pockets: 9 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein CT_858	protein	522	35% helix, 22% strand	O84866
B	Protein CT_858	protein	527	35% helix, 21% strand	O84866

Ligands and binding sites

SO4 · Sulfate ion · ion · 15 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	853	0.79	0.82	79	SO4
2	650	0.73	0.80	46	empty
3	329	0.69	0.82	43	SO4
4	258	0.55	0.77	34	empty
5	230	0.53	0.76	30	empty

Interfaces

1 interface between chains.

A–B · 2283 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

3DOR · Crystal Structure of mature CPAF · the same entry in another collection · chain A against A, TM-score 1.00
O84866 · AlphaFold monomer V2.0 prediction for protein CT_858 (O84866) · a predicted model of the same protein · chain A against A, TM-score 0.99

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O84866
Elsewhere: RCSB PDB 3DOR · PDBe 3DOR · UniProt O84866

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