MolNFT v1 · #88171 · protein

X-ray analyses of aspartic proteinases IV. structure and refinement at 2.2 ångströms resolution of bovine chymosin

4CMS · Chymosin B: “X-ray analyses of aspartic proteinases IV. structure and refinement at 2.2 ångströms resolution of bovine…”. X-ray diffraction, 2 pockets (best druggability 0.43). MolNFT v1 #88171 on GenesisL1: 3D structure, binding…

PDB: 4CMS
Type: protein
Length: 320 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chymosin B
EC: 3.4.23.4
UniProt: P00794
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chymosin B (EC 3.4.23.4)	protein	320	15% helix, 49% strand	P00794

Pockets

2 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	157	0.43	0.74	27	empty
2	122	0.43	0.77	20	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

4CMS · X-ray analyses of aspartic proteinases IV. structure and refinement at 2.2 ångströms… · the same entry in another collection · chain A against A, TM-score 1.00
P00794 · AlphaFold monomer V2.0 prediction for chymosin (P00794) · 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 P00794
Elsewhere: RCSB PDB 4CMS · PDBe 4CMS · UniProt P00794

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