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Aquifex aeolicus mutl ATPase domain complexed with amppcp

Analyse Aquifex aeolicus mutl ATPase domain complexed with amppcp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LZJ
Type: protein
Length: 245 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA mismatch repair protein mutl
UniProt: O67518
Ligands: ACP, MG
Pockets: 3 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA mismatch repair protein mutl	protein	245	32% helix, 33% strand	O67518

Ligands and binding sites

ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

3 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	105	0.41	0.77	18	ACP
2	58	0.28	0.74	13	empty
3	52	0.27	0.74	14	empty

Compared structures

6LZJ · Aquifex aeolicus MutL ATPase domain complexed with AMPPCP · 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 0.98

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

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