MolNFT v1 · #115818 · protein

Crystal structure of semet-substituted N-terminal truncated human B12- chaperone cbld (108-296)

5CUZ · Methylmalonic aciduria and homocystinuria type D protein…: “Crystal structure of semet-substituted N-terminal truncated human B12- chaperone cbld (108-296)”. X-ray diffraction, 1 pocket (best druggability 0.48). MolNFT v1 #115818 on…

PDB: 5CUZ
Type: protein
Length: 158 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methylmalonic aciduria and homocystinuria type D protein, mitochondrial
UniProt: Q9H3L0
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methylmalonic aciduria and homocystinuria type D protein, mitochondrial	protein	158	29% helix, 24% strand	Q9H3L0

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	88	0.48	0.82	21	empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

5CUZ · Crystal structure of SeMet-substituted N-terminal truncated human B12-chaperone CblD… · the same entry in another collection · chain A against A, TM-score 1.00
Q9H3L0 · AlphaFold monomer V2.0 prediction for cobalamin trafficking protein cbld (Q9H3L0) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q9H3L0
Elsewhere: RCSB PDB 5CUZ · PDBe 5CUZ · UniProt Q9H3L0

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