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4H4F

Crystal structure of human chymotrypsin C (CTRC) bound to inhibitor eglin c from Hirudo medicinalis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0006508biological_processproteolysis
A0006874biological_processintracellular calcium ion homeostasis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0009611biological_processresponse to wounding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 301
ChainResidue
AARG175
AARG218
ALYS224
AHOH515
AHOH575
AHOH594
BGLY40

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 302
ChainResidue
ALYS178
AHOH628
AHOH637
AARG100
ALYS177

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 101
ChainResidue
ATYR35
ALYS36
AARG62
BARG48
BTYR49
BASN50
BARG51
BHOH231

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SAcnGDSGGPLN
ChainResidueDetails
ASER189-ASN200

site_idPS00285
Number of Residues12
DetailsPOTATO_INHIBITOR Potato inhibitor I family signature. FPEVVGktVdqA
ChainResidueDetails
BPHE10-ALA21

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
QASN9
AASP102
ASER195

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN36
AASN204

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PDB entries from 2024-07-17

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