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3BQU

Crystal Structure of the 2F5 Fab'-3H6 Fab Complex

Functional Information from GO Data
ChainGOidnamespacecontents
C0002250biological_processadaptive immune response
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005886cellular_componentplasma membrane
C0030183biological_processB cell differentiation
C0042105cellular_componentalpha-beta T cell receptor complex
C0071735cellular_componentIgG immunoglobulin complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 225
ChainResidue
CARG55
DTYR32
DARG98
DSER100
DILE101
DPRO110

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. CVSDSGAETTVT
ChainResidueDetails
CCYS-6-THR5

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCNVNH
ChainResidueDetails
BTYR213-HIS219
ATYR192-HIS198
CTYR192-HIS198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine; atypical","evidences":[{"source":"PubMed","id":"6816276","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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