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Pectobacterium phage ZF40 apo-ACA2

Analyse Pectobacterium phage ZF40 apo-ACA2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7VJO
Type: protein
Length: 235 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Anti-CRISPR-associated protein ACA2
UniProt: H9C180
Ligands: MG, CL
Pockets: 3 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 66% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Anti-CRISPR-associated protein ACA2	protein	118	65% helix, 3% strand	H9C180
A	Anti-CRISPR-associated protein ACA2	protein	117	66% helix, 3% strand	H9C180

Ligands and binding sites

MG · Magnesium ion · metal · 4 copies · chains B, A
CL · Chloride ion · ion · 2 copies · chains B, 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	92	0.41	0.78	17	empty
2	131	0.38	0.73	19	CL
3	81	0.33	0.74	13	empty

Interfaces

1 interface between chains.

B–A · 1256 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

7VJO · Pectobacterium phage ZF40 apo-Aca2 · the same entry in another collection · chain B against B, 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 H9C180
Elsewhere: RCSB PDB 7VJO · PDBe 7VJO · UniProt H9C180

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