MolNFT v1 · #81347 · protein

Bond length analysis of asp, glu and his residues in subtilisin carlsberg at 1.26A resolution

3UNX: “Bond length analysis of asp, glu and his residues in subtilisin carlsberg at 1.26A resolution”. X-ray diffraction, 2 ligands (CA, NA), 1 pocket (best druggability 0.38). MolNFT v1 #81347 on GenesisL1: 3D structure, binding sites and…

PDB: 3UNX
Type: protein
Length: 274 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Subtilisin carlsberg
EC: 3.4.21.62
UniProt: P00780
Ligands: CA, NA
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Subtilisin carlsberg (EC 3.4.21.62)	protein	274	30% helix, 20% strand	P00780

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A
NA · Sodium ion · metal · chains A
GOL · Glycerol · additive · 4 copies · chains A

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

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	105	0.38	0.75	34	GOL

Compared structures

3UNX · Bond length analysis of asp, glu and his residues in subtilisin Carlsberg at 1.26A… · the same entry in another collection · chain A against A, TM-score 1.00
P00780 · AlphaFold monomer V2.0 prediction for subtilisin carlsberg (P00780) · a predicted model of the same protein · 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 P00780
Elsewhere: RCSB PDB 3UNX · PDBe 3UNX · UniProt P00780

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