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1NUF

Role of Calcium Ions in the Activation and Activity of the Transglutaminase 3 Enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0003810molecular_functionprotein-glutamine gamma-glutamyltransferase activity
A0003824molecular_functioncatalytic activity
A0005198molecular_functionstructural molecule activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0018149biological_processpeptide cross-linking
A0030216biological_processkeratinocyte differentiation
A0031069biological_processhair follicle morphogenesis
A0031234cellular_componentextrinsic component of cytoplasmic side of plasma membrane
A0031424biological_processkeratinization
A0032991cellular_componentprotein-containing complex
A0036211biological_processprotein modification process
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 701
ChainResidue
AASN430
AGLN669

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 702
ChainResidue
AARG169
AARG587
AILE590

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 703
ChainResidue
AASP183
ASER186

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 705
ChainResidue
AARG291

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 706
ChainResidue
AASN224
AASN226
AASP227
AASN229
AALA221

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR A 707
ChainResidue
ATRP236

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR A 708
ChainResidue
AASN226
AASP227

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR A 709
ChainResidue
ALEU638

Functional Information from PROSITE/UniProt
site_idPS00547
Number of Residues18
DetailsTRANSGLUTAMINASES Transglutaminases active site. GQCWVfAGTlnTaLRSLG
ChainResidueDetails
AGLY270-GLY287

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10024","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11980702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12679341","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Bensaad K.","Vousden K.H."]}}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1g0d
ChainResidueDetails
AASP353
ACYS272
ATYR525
AHIS330

250835

PDB entries from 2026-03-18

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