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

1EMO

NMR STUDY OF A PAIR OF FIBRILLIN CA2+ BINDING EPIDERMAL GROWTH FACTOR-LIKE DOMAINS, 22 STRUCTURES

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 2224
ChainResidue
AASP2127
AMET2128
AGLU2130
AASN2144
ATHR2145
ASER2148

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 2225
ChainResidue
AASP2166
ATHR2167
AGLU2169
AASN2183
AVAL2184
AGLY2187

site_idCA1
Number of Residues6
DetailsCALCIUM BINDING SITE FOR EGF-LIKE DOMAIN 32.
ChainResidue
AASP2127
AASP2129
AGLU2130
AASN2144
ATYR2149
ACA2224

site_idCA2
Number of Residues6
DetailsCALCIUM BINDING SITE FOR EGF-LIKE DOMAIN 33.
ChainResidue
AASN2183
APHE2188
ACA2225
AASP2166
AASP2168
AGLU2169

Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiNtdgsYrCeC
ChainResidueDetails
ACYS2142-CYS2153
ACYS2181-CYS2192

site_idPS01186
Number of Residues14
DetailsEGF_2 EGF-like domain signature 2. CeCpfGYilagne..C
ChainResidueDetails
ACYS2151-CYS2164
ACYS2190-CYS2204

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DmDECkepdv.........Ckhgq...CiNtdgsYrC
ChainResidueDetails
AASP2127-CYS2151
AASP2166-CYS2190

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues38
DetailsDomain: {"description":"EGF-like 36; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues39
DetailsDomain: {"description":"EGF-like 37; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Glc) serine","evidences":[{"source":"PubMed","id":"34411563","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon