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1HA9

SOLUTION STRUCTURE OF THE SQUASH TRYPSIN INHIBITOR MCoTI-II, NMR, 30 STRUCTURES.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005576cellular_componentextracellular region
A0006952biological_processdefense response
A0030414molecular_functionpeptidase inhibitor activity
A1900004biological_processnegative regulation of serine-type endopeptidase activity
Functional Information from PROSITE/UniProt
site_idPS00286
Number of Residues20
DetailsSQUASH_INHIBITOR Squash family of serine protease inhibitors signature. CPkilkkCrrDsDCpgaCiC
ChainResidueDetails
ACYS8-CYS27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive bond
ChainResidueDetails
ALYS10

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: Cyclopeptide (Ser-Gly) => ECO:0000269|PubMed:10801322
ChainResidueDetails
ASER1
AGLY34

site_idSWS_FT_FI3
Number of Residues2
DetailsCROSSLNK: Isoaspartyl glycine isopeptide (Asp-Gly); alternate => ECO:0000269|PubMed:10801322
ChainResidueDetails
AASP4
AGLY5

218853

PDB entries from 2024-04-24

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