MolNFT v1 · #38103 · protein

Three-dimensional structure of chymotrypsin inactivated with (2S) N- acetyl-L-alanyl-L-phenylalanyl-chloroethyl ketone: implications for the mechanism of inactivation of serine proteases by chloroketones

2GMT: “Three-dimensional structure of chymotrypsin inactivated with (2S) N…”. X-ray diffraction. MolNFT v1 #38103 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2GMT
Type: protein
Length: 236 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P00766

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	10	—	P00766
B	—	protein	131	—	P00766
C	—	protein	95	—	P00766

Compared structures

2GMT · Three-dimensional structure of chymotrypsin inactivated with (2S)… · the same entry in another collection · chain A against A, TM-score 1.00
P00766 · AlphaFold monomer V2.0 prediction for chymotrypsinogen a (P00766) · a predicted model of the same protein · chain C against A, TM-score 0.99

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 P00766
Elsewhere: RCSB PDB 2GMT · PDBe 2GMT · UniProt P00766

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