MolNFT v1 · #93483 · protein

Crystal structure of CRISPR-associated protein CSE1 from acidimicrobium ferrooxidans

4H3T · CRISPR-associated protein, CSE1 family: “Crystal structure of CRISPR-associated protein CSE1 from acidimicrobium ferrooxidans”. X-ray diffraction, 4 pockets (best druggability 0.68). MolNFT v1 #93483 on GenesisL1: 3D structure…

PDB: 4H3T
Type: protein
Length: 517 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CRISPR-associated protein, CSE1 family
UniProt: C7LYW9
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CRISPR-associated protein, CSE1 family	protein	517	44% helix, 19% strand	C7LYW9

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.68	0.95	25	GOL
2	59	0.59	0.91	19	GOL
3	138	0.50	0.79	28	empty
4	68	0.37	0.78	16	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

4H3T · Crystal structure of CRISPR-associated protein Cse1 from Acidimicrobium ferrooxidans · 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 C7LYW9
Elsewhere: RCSB PDB 4H3T · PDBe 4H3T · UniProt C7LYW9

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