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1G1R

Crystal structure of P-selectin lectin/EGF domains complexed with SLeX

Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CsCypGfyGPeC
ChainResidueDetails
ACYS142-CYS153

site_idPS00615
Number of Residues28
DetailsC_TYPE_LECTIN_1 C-type lectin domain signature. CVeiyikspsapgkWNDEHClkkkh.ALC
ChainResidueDetails
ACYS90-CYS117

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CsCypGFygpe....C
ChainResidueDetails
ACYS142-CYS153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:11081633, ECO:0007744|PDB:1G1Q, ECO:0007744|PDB:1G1R
ChainResidueDetails
AGLU80
CASN82
CASN105
CASP106
DGLU80
DASN82
DASN105
DASP106
AASN82
AASN105
AASP106
BGLU80
BASN82
BASN105
BASP106
CGLU80

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:1G1R
ChainResidueDetails
AASN83
BASN83
CASN83
DASN83

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11081633, ECO:0007744|PDB:1G1R
ChainResidueDetails
AGLU92
BGLU92
CGLU92
DGLU92

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16263699
ChainResidueDetails
AASN13
BASN13
CASN13
DASN13

site_idSWS_FT_FI5
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN57
AASN139
BASN57
BASN139
CASN57
CASN139
DASN57
DASN139

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PDB entries from 2024-07-17

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