MolNFT v1 · #32552 · protein

Crystal structure of ALR0975

2BTW · ALR0975 protein: “Crystal structure of ALR0975”. X-ray diffraction, 1 ligand (CA), 4 pockets (best druggability 0.68). MolNFT v1 #32552 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2BTW
Type: protein
Length: 420 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALR0975 protein
EC: 2.3.2.15
UniProt: Q8YY76
Ligands: CA
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ALR0975 protein (EC 2.3.2.15)	protein	210	39% helix, 20% strand	Q8YY76
B	ALR0975 protein (EC 2.3.2.15)	protein	210	40% helix, 20% strand	Q8YY76

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	463	0.68	0.79	61	empty
2	141	0.41	0.75	33	empty
3	67	0.37	0.79	17	empty
4	69	0.34	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 1206 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

2BTW · Crystal structure of Alr0975 · the same entry in another collection · chain A against A, TM-score 1.00

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 Q8YY76
Elsewhere: RCSB PDB 2BTW · PDBe 2BTW · UniProt Q8YY76

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