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Crystal structure of a putative ssrna endonuclease CAS2, CRISPR adaptation protein from E.COLI

Analyse Crystal structure of a putative ssrna endonuclease CAS2, CRISPR adaptation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MAK
Type: protein
Length: 149 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CRISPR-associated endoribonuclease CAS2
EC: 3.1.-.-
UniProt: P45956

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CRISPR-associated endoribonuclease CAS2 (EC 3.1.-.-)	protein	73	33% helix, 40% strand	P45956
B	CRISPR-associated endoribonuclease CAS2 (EC 3.1.-.-)	protein	76	32% helix, 39% strand	P45956

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · chains A, B

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

Interfaces

1 interface between chains.

A–B · 866 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4MAK · Crystal structure of a putative ssRNA endonuclease Cas2, CRISPR adaptation protein from… · the same entry in another collection · chain A against A, TM-score 1.00
P45956 · AlphaFold monomer V2.0 prediction for CRISPR-associated endoribonuclease CAS2 (P45956) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P45956
Elsewhere: RCSB PDB 4MAK · PDBe 4MAK · UniProt P45956

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