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5VPL

CRYSTAL STRUCTURE OF DER F 1 COMPLEXED WITH FAB 4C1

Replaces:  3RVV
Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
C0002250biological_processadaptive immune response
C0002376biological_processimmune system process
C0005576cellular_componentextracellular region
C0005886cellular_componentplasma membrane
C0019814cellular_componentimmunoglobulin complex
Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGgCGSCWAfSG
ChainResidueDetails
AGLN29-GLY40

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
CTYR192-HIS198

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. NYHAVNIVGYG
ChainResidueDetails
AASN169-GLY179

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvRNSWdttWGdsGYGyF
ChainResidueDetails
ATYR186-PHE205

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19136006","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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