MolNFT v1 · #56727 · protein

X-ray crystal structure of a CRISPR-associated CMR5 family protein from thermus thermophilus HB8

2ZOP · Putative uncharacterized protein TTHB164: “X-ray crystal structure of a CRISPR-associated CMR5 family protein from thermus thermophilus HB8”. X-ray diffraction, 1 ligand (SO4), 7 pockets (best druggability 0.46). MolNFT v1 #56727 on…

PDB: 2ZOP
Type: protein
Length: 662 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein TTHB164
UniProt: Q53W05
Ligands: SO4
Pockets: 7 · best druggability 0.46

Structure

x-ray diffraction · 6 distinct chains · 83% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein TTHB164	protein	113	81% helix, 0% strand	Q53W05
B	Putative uncharacterized protein TTHB164	protein	112	83% helix, 0% strand	Q53W05
C	Putative uncharacterized protein TTHB164	protein	108	83% helix, 0% strand	Q53W05
D	Putative uncharacterized protein TTHB164	protein	107	83% helix, 0% strand	Q53W05
E	Putative uncharacterized protein TTHB164	protein	111	83% helix, 0% strand	Q53W05
F	Putative uncharacterized protein TTHB164	protein	111	83% helix, 0% strand	Q53W05

Ligands and binding sites

SO4 · Sulfate ion · ion · 7 copies · chains A, B, C, F

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

Pockets

7 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	192	0.46	0.75	27	empty
2	141	0.38	0.72	22	empty
3	91	0.34	0.74	21	empty
4	91	0.33	0.73	19	empty
5	62	0.27	0.73	18	empty

Interfaces

8 interfaces between chains.

C–F · 343 Å² buried · 11 hydrogen bonds · protein-protein
D–F · 301 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 287 Å² buried · 0 hydrogen bonds · protein-protein
E–F · 276 Å² buried · 0 hydrogen bonds · protein-protein
A–C · 275 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

2ZOP · X-ray crystal structure of a CRISPR-associated Cmr5 family protein from Thermus… · the same entry in another collection · chain F against F, TM-score 1.00
Q53W05 · AlphaFold monomer V2.0 prediction for CRISPR system cmr subunit CMR5 (Q53W05) · a predicted model of the same protein · chain F against A, TM-score 0.99

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 Q53W05
Elsewhere: RCSB PDB 2ZOP · PDBe 2ZOP · UniProt Q53W05

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.