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2ZGH

Crystal Structure of active granzyme M bound to its product

Functional Information from GO Data
ChainGOidnamespacecontents
A0001913biological_processT cell mediated cytotoxicity
A0002376biological_processimmune system process
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0006915biological_processapoptotic process
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0031640biological_processkilling of cells of another organism
A0045087biological_processinnate immune response
A0051604biological_processprotein maturation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 241
ChainResidue
ATHR128
ASER135
AARG136
AVAL137
AARG139

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 242
ChainResidue
ALYS173
AHOH296
AGLN45
AARG46
AMET47
AALA48

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 243
ChainResidue
AARG51
AHIS67
AHOH359

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 244
ChainResidue
ALYS34
AGLN91
AARG203
AHOH375
AHOH409

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 245
ChainResidue
AGLY189
ALYS190
AHOH397

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU37-CYS42

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. APckGDSGGPLV
ChainResidueDetails
AALA176-VAL187

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues228
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"19542453","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER182
AASP86
AHIS41

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER182
AGLY183
AASP86
AHIS41

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP86
AHIS41

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY180
ASER182

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER182
AGLY183

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY180
ASER182
AASP86
AHIS41

239149

PDB entries from 2025-07-23

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