MolNFT v1 · #1581 · protein

Mutl complexed with adpnp

1B63: “Mutl complexed with adpnp”. X-ray diffraction, 2 ligands (ANP, MG), 3 pockets (best druggability 0.72). MolNFT v1 #1581 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1B63
Type: protein
Length: 333 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mutl
UniProt: P23367
Ligands: ANP, MG
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mutl	protein	333	37% helix, 26% strand	P23367

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
MG · Magnesium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 2 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	272	0.72	0.86	37	MG, ANP
2	202	0.55	0.78	37	EDO
3	143	0.50	0.79	23	empty

Compared structures

1B63 · Mutl complexed with adpnp · the same entry in another collection · chain A against A, TM-score 1.00
P23367 · AlphaFold monomer V2.0 prediction for DNA mismatch repair protein mutl (P23367) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P23367
Elsewhere: RCSB PDB 1B63 · PDBe 1B63 · UniProt P23367

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