MolNFT v1 · #105724 · protein

Crystal structure of CMR4

4RDP · CRISPR system cmr subunit CMR4: “Crystal structure of CMR4”. X-ray diffraction, 5 pockets (best druggability 0.74). MolNFT v1 #105724 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4RDP
Type: protein
Length: 498 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CRISPR system cmr subunit CMR4
UniProt: Q8U1S9
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CRISPR system cmr subunit CMR4	protein	250	32% helix, 29% strand	Q8U1S9
B	CRISPR system cmr subunit CMR4	protein	248	34% helix, 29% strand	Q8U1S9

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	85	0.74	0.96	26	empty
2	340	0.66	0.81	30	empty
3	302	0.59	0.77	27	empty
4	80	0.44	0.80	14	empty
5	98	0.39	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 1476 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

4RDP · Crystal structure of Cmr4 · the same entry in another collection · chain A against A, TM-score 1.00
Q8U1S9 · AlphaFold monomer V2.0 prediction for CRISPR system cmr endoribonuclease CMR4 (Q8U1S9) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q8U1S9
Elsewhere: RCSB PDB 4RDP · PDBe 4RDP · UniProt Q8U1S9

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