MolNFT v1 · #3664 · protein

Chymosin complex with the inhibitor cp-113972

1CZI: “Chymosin complex with the inhibitor cp-113972”. X-ray diffraction, 1 pocket (best druggability 0.40). MolNFT v1 #3664 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1CZI
Type: protein
Length: 327 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chymosin; Cp-113972 (norstatine-S-methyl cysteine-iodo-phenylalanine- proline)
EC: 3.4.23.4
UniProt: P00794
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Chymosin (EC 3.4.23.4)	protein	323	12% helix, 49% strand	P00794
P	Cp-113972 (norstatine-S-methyl cysteine-iodo-phenylalanine- proline)	protein	4	0% helix, 0% strand	—

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	114	0.40	0.76	27	empty

Interfaces

1 interface between chains.

E–P · 596 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide, 3 modified (disulfide, nonstandard, methylation).

Compared structures

1CZI · Chymosin complex with the inhibitor cp-113972 · the same entry in another collection · chain E against E, TM-score 1.00
P00794 · AlphaFold monomer V2.0 prediction for chymosin (P00794) · a predicted model of the same protein · chain E against A, TM-score 0.97

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 1CZI · PDBe 1CZI · UniProt P00794

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