Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5VPH

CRYSTAL STRUCTURE OF DER P 1 COMPLEXED WITH FAB 4C1

Replaces:  3RVX
Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 301
ChainResidue
AASP56
ALEU57
AGLU59
AGLU91
AEDO302
AHOH428

site_idAC2
Number of Residues7
Detailsbinding site for residue EDO A 302
ChainResidue
AGLU59
AGLU91
ACA301
AHOH435
AARG26
AMET27
AASP56

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGgCGSCWAfSG
ChainResidueDetails
AGLN28-GLY39

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. NYHAVNIVGYS
ChainResidueDetails
AASN168-SER178

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvRNSWdtnWGdnGYGyF
ChainResidueDetails
ATYR185-PHE204

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ACYS34
AHIS170
AASN190

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16148130
ChainResidueDetails
AASN52

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon