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8OXV

Transglutaminase 3 zymogen in complex with DH patient-derived Fab DH63-B02

Functional Information from GO Data
ChainGOidnamespacecontents
A0003810molecular_functionprotein-glutamine gamma-glutamyltransferase activity
A0003824molecular_functioncatalytic activity
A0005198molecular_functionstructural molecule activity
A0005509molecular_functioncalcium ion 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 PROSITE/UniProt
site_idPS00547
Number of Residues18
DetailsTRANSGLUTAMINASES Transglutaminases active site. GQCWVfAGTlnTaLRSLG
ChainResidueDetails
AGLY271-GLY288

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
ChainResidueDetails
BTYR203-HIS209
CTYR195-HIS201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024
ChainResidueDetails
ACYS273
AHIS331
AASP354

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:11980702, ECO:0000269|PubMed:12679341
ChainResidueDetails
AALA222
AASN225
AASN227
AASP228
AASN230
AASP302
AASP304
AASN306
ASER308
AASP325
AASN394
ASER416
AGLU444
AGLU449

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Cleavage; by CTSL
ChainResidueDetails
AALA467

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.7
ChainResidueDetails
AALA2

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR111

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATHR112

219869

PDB entries from 2024-05-15

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