MolNFT v1 · #166544 · protein

Cryo-EM structure of the escherichia COLI mcrbc complex

6UT6: “Cryo-EM structure of the escherichia COLI mcrbc complex”. Electron microscopy, 3 ligands (GSP, GDP, MG). MolNFT v1 #166544 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6UT6
Type: protein
Length: 2,078 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P15005, P15006
Ligands: GSP, GDP, MG

Structure

electron microscopy · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	—	protein	288	—	P15005
C	—	protein	287	—	P15005
D, E, F	—	protein	292	—	P15005
G	—	protein	339	—	P15006

Ligands and binding sites

GSP · 5'-guanosine-diphosphate-monothiophosphate · ligand · 5 copies · chains B, C, D, E, F, A
GDP · Guanosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · 4 copies · chains B, C, D, E

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

Compared structures

6UT6 · Cryo-EM structure of the Escherichia coli McrBC complex · the same entry in another collection · chain G against G, TM-score 1.00
P15005 · AlphaFold monomer V2.0 prediction for 5-methylcytosine-specific restriction enzyme B… · a predicted model of the same protein · chain D against A, TM-score 0.99
P15006 · AlphaFold monomer V2.0 prediction for protein mcrc (P15006) · a predicted model of the same protein · chain G against A, TM-score 0.90

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 P15005
Every structure of UniProt P15006
Elsewhere: RCSB PDB 6UT6 · PDBe 6UT6 · UniProt P15005 · UniProt P15006

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