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2OUH

Crystal structure of the Thrombospondin-1 N-terminal domain in complex with fractionated Heparin DP10

Functional Information from GO Data
ChainGOidnamespacecontents
A0005615cellular_componentextracellular space
A0008201molecular_functionheparin binding
A0016525biological_processnegative regulation of angiogenesis
A0050840molecular_functionextracellular matrix binding
B0005615cellular_componentextracellular space
B0008201molecular_functionheparin binding
B0016525biological_processnegative regulation of angiogenesis
B0050840molecular_functionextracellular matrix binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 248
ChainResidue
AARG29
AVAL31
AARG42
AARG77
AHOH281

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 249
ChainResidue
AHOH310
AARG42
AARG77
AMET79
AGLY133

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 250
ChainResidue
BLYS24
BPRO51
BHOH265

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 248
ChainResidue
BVAL31
BARG42
BVAL193

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 249
ChainResidue
BARG42
BGLU44

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 250
ChainResidue
BARG42
BGLN78
BMET79
BGLN191
BGLY192

Functional Information from PROSITE/UniProt
site_idPS00414
Number of Residues9
DetailsPROFILIN Profilin signature. rSpWNrIpE
ChainResidueDetails
AARG-3-GLU5

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:16263699, ECO:0000305|PubMed:16335952, ECO:0000305|PubMed:18065761
ChainResidueDetails
AASN230
BASN230

237735

PDB entries from 2025-06-18

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