MolNFT v1 · #156300 · protein

Aquifex aeolicus mutl ATPase domain complexed with ADP

6LZI · DNA mismatch repair protein mutl: “Aquifex aeolicus mutl ATPase domain complexed with ADP”. X-ray diffraction, 2 ligands (ADP, MG), 2 pockets (best druggability 0.43). MolNFT v1 #156300 on GenesisL1: 3D structure, binding sites and…

PDB: 6LZI
Type: protein
Length: 240 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA mismatch repair protein mutl
UniProt: O67518
Ligands: ADP, MG
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA mismatch repair protein mutl	protein	240	32% helix, 34% strand	O67518

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
PEG · Di(hydroxyethyl)ether · additive · 5 copies · chains A

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

Pockets

2 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	103	0.43	0.78	20	MG, ADP
2	75	0.31	0.74	15	empty

Compared structures

6LZI · Aquifex aeolicus MutL ATPase domain complexed with ADP · the same entry in another collection · chain A against A, TM-score 1.00
O67518 · AlphaFold monomer V2.0 prediction for DNA mismatch repair protein mutl (O67518) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 O67518
Elsewhere: RCSB PDB 6LZI · PDBe 6LZI · UniProt O67518

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