MolNFT v1 · #182142 · protein + DNA

Symmetrical pam-pam prespacer bound CAS4/CAS1/CAS2 complex

7MI4: “Symmetrical pam-pam prespacer bound CAS4/CAS1/CAS2 complex”. Electron microscopy, 2 ligands (SF4, MN). MolNFT v1 #182142 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7MI4
Type: protein + DNA
Length: 2,048 residues
Chains: 8
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q74H36, Q74H35
Ligands: SF4, MN

Structure

electron microscopy · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	—	protein	554	—	Q74H36
B, D	—	protein	340	—	Q74H36
E, F	—	protein	95	—	Q74H35
G, H	—	dna	35	—	—

Ligands and binding sites

SF4 · Iron/sulfur cluster · ligand · 2 copies · chains A, C
MN · Manganese (II) ion · metal · 8 copies · chains A, B, C, G, D, E, H, F

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

Compared structures

7MI4 · Symmetrical PAM-PAM prespacer bound Cas4/Cas1/Cas2 complex · the same entry in another collection · chain H against H, TM-score 1.00
Q74H36 · AlphaFold monomer V2.0 prediction for CRISPR-associated exonuclease CAS4/ENDONUCLEASE… · a predicted model of the same protein · chain A against A, TM-score 0.97
Q74H35 · AlphaFold monomer V2.0 prediction for CRISPR-associated endoribonuclease CAS2 (Q74H35) · a predicted model of the same protein · chain E against A, TM-score 0.86

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 Q74H36
Every structure of UniProt Q74H35
Elsewhere: RCSB PDB 7MI4 · PDBe 7MI4 · UniProt Q74H36 · UniProt Q74H35

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