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Crystal structure of a putative CAS1 enzyme from vibrio phage ICP1

Analyse Crystal structure of a putative CAS1 enzyme from vibrio phage ICP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4W8K
Type: protein
Length: 586 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CAS1 protein
UniProt: F1D4K1
Ligands: K
Pockets: 5 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 54% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CAS1 protein	protein	289	56% helix, 13% strand	F1D4K1
B	CAS1 protein	protein	297	52% helix, 13% strand	F1D4K1

Ligands and binding sites

K · Potassium ion · metal · chains B

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

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	148	0.81	0.97	26	empty
2	288	0.70	0.85	37	empty
3	451	0.64	0.77	42	empty
4	96	0.40	0.77	18	empty
5	98	0.34	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 1919 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

4W8K · Crystal structure of a putative Cas1 enzyme from Vibrio phage ICP1 · the same entry in another collection · chain A against A, 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 F1D4K1
Elsewhere: RCSB PDB 4W8K · PDBe 4W8K · UniProt F1D4K1

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