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

6BDZ

ADAM10 Extracellular Domain Bound by the 11G2 Fab

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TFAHEVGHNF
ChainResidueDetails
ATHR380-PHE389

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
LTYR215-HIS221

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:29224781, ECO:0000269|PubMed:29430990
ChainResidueDetails
AGLU384

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:24055016, ECO:0000269|PubMed:29224781, ECO:0000269|PubMed:37516108, ECO:0007744|PDB:6BDZ, ECO:0007744|PDB:6BE6, ECO:0007744|PDB:8ESV
ChainResidueDetails
AHIS383
AHIS393

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:29224781, ECO:0000269|PubMed:37516108, ECO:0007744|PDB:6BE6, ECO:0007744|PDB:8ESV
ChainResidueDetails
AHIS387

site_idSWS_FT_FI4
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AGLN267
AGLN439
AGLN551

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:29224781, ECO:0007744|PDB:6BDZ, ECO:0007744|PDB:6BE6
ChainResidueDetails
AASN278

225158

PDB entries from 2024-09-18

PDB statisticsPDBj update infoContact PDBjnumon