Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7MYZ

Structure of the full length 5-TM receptor CD47 bound to Fab B6H12

Functional Information from GO Data
ChainGOidnamespacecontents
C0005506molecular_functioniron ion binding
C0005886cellular_componentplasma membrane
C0009055molecular_functionelectron transfer activity
C0020037molecular_functionheme binding
C0022409biological_processpositive regulation of cell-cell adhesion
C0022900biological_processelectron transport chain
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
C0050729biological_processpositive regulation of inflammatory response
C0050766biological_processpositive regulation of phagocytosis
C0070053molecular_functionthrombospondin receptor activity
D0005506molecular_functioniron ion binding
D0005886cellular_componentplasma membrane
D0009055molecular_functionelectron transfer activity
D0020037molecular_functionheme binding
D0022409biological_processpositive regulation of cell-cell adhesion
D0022900biological_processelectron transport chain
D0042597cellular_componentperiplasmic space
D0046872molecular_functionmetal ion binding
D0050729biological_processpositive regulation of inflammatory response
D0050766biological_processpositive regulation of phagocytosis
D0070053molecular_functionthrombospondin receptor activity
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
LTYR192-HIS198
HTYR199-HIS205

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues284
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
CGLN1-GLU123
CVAL180-ALA189
CSER239-GLY250
DGLN1-GLU123
DVAL286-ALA295
DSER345-GLY356

site_idSWS_FT_FI2
Number of Residues200
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
CASN124-ILE144
DPRO357-MET377
CILE159-PHE179
CTHR190-PHE210
CSER218-LEU238
CPRO251-MET271
DASN124-ILE144
DILE265-PHE285
DTHR296-PHE316
DSER324-LEU344

site_idSWS_FT_FI3
Number of Residues78
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
CSER211-THR217
CLYS272-GLU305
DSER317-THR323
DLYS378-GLU411

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:18657508
ChainResidueDetails
CGLN1
DGLN1

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P97829
ChainResidueDetails
CSER71
DSER71

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18657508
ChainResidueDetails
CASN5
DASN5

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
CASN16
DASN16

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18657508, ECO:0000269|PubMed:19349973
ChainResidueDetails
CASN32
DASN32

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18657508, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
ChainResidueDetails
CASN55
DASN55

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18657508, ECO:0000269|PubMed:19159218
ChainResidueDetails
CASN93
DASN93

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CASN188
DASN294

site_idSWS_FT_FI12
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
CTRP147
CILE151
DTRP159
DILE254

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon