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A second active site in chymotrypsin? the X-ray crystal structure of N-acetyl-D-tryptophan bound to gamma-chymotrypsin

Analyse A second active site in chymotrypsin? the X-ray crystal structure of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GHA
Type: protein
Length: 240 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P00766

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	—	protein	10	—	P00766
F	—	protein	131	—	P00766
G	—	protein	95	—	P00766
P	—	protein	4	—	—

Compared structures

1GHA · A second active site in chymotrypsin? the X-ray crystal structure of… · the same entry in another collection · chain F against F, TM-score 1.00
P00766 · AlphaFold monomer V2.0 prediction for chymotrypsinogen a (P00766) · a predicted model of the same protein · chain G 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 1GHA · PDBe 1GHA · UniProt P00766

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