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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
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
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024
ChainResidueDetails
ACYS272
AHIS330
AASP353

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:11980702, ECO:0000269|PubMed:12679341
ChainResidueDetails
AALA221
AASP324
AASN393
ASER415
AGLU443
AGLU448
AASN224
AASN226
AASP227
AASN229
AASP301
AASP303
AASN305
ASER307

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Cleavage; by CTSL
ChainResidueDetails
AALA466

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.7
ChainResidueDetails
AALA1

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR110

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATHR111

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

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PDB entries from 2024-07-24

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