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1TYE

Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen

Functional Information from GO Data
ChainGOidnamespacecontents
A0007155biological_processcell adhesion
A0008305cellular_componentintegrin complex
C0007155biological_processcell adhesion
C0008305cellular_componentintegrin complex
E0007155biological_processcell adhesion
E0008305cellular_componentintegrin complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
ChainResidueDetails
BSER121
AASP305
AASP365
AASP367
AASP369
ATYR371
AASP373
AASP426
AASP428
AASN430
ATYR432
BGLU220
AASP434
CGLU243
CASP245
CASP247
CTHR250
CGLU252
CASP297
CASN299
CASP301
CARG303
DSER121
CASP305
CASP365
CASP367
CASP369
CTYR371
CASP373
CASP426
CASP428
CASN430
CTYR432
DGLU220
CASP434
EGLU243
EASP245
EASP247
ETHR250
EGLU252
EASP297
EASN299
EASP301
EARG303
FSER121
EASP305
EASP365
EASP367
EASP369
ETYR371
EASP373
EASP426
EASP428
EASN430
ETYR432
FGLU220
EASP434
AASN299
AASP301
AARG303

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCU
ChainResidueDetails
BSER123
DSER123
FSER123

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: in ADMIDAS binding site => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU, ECO:0007744|PDB:3IJE
ChainResidueDetails
BASP126
BASP127
DASP126
DASP127
FASP126
FASP127

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: in LIMBS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
ChainResidueDetails
BASP158
FASN215
FASP217
FPRO219
BASN215
BASP217
BPRO219
DASP158
DASN215
DASP217
DPRO219
FASP158

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: in LIMBS binding site => ECO:0007744|PDB:4G1M
ChainResidueDetails
BASP251
DASP251
FASP251

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3IJE
ChainResidueDetails
BMET335
DMET335
FMET335

site_idSWS_FT_FI7
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3IJE
ChainResidueDetails
BASN99
DASN99
FASN99

site_idSWS_FT_FI8
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3IJE
ChainResidueDetails
BASN320
BASN371
DASN320
DASN371
FASN320
FASN371

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PDB entries from 2024-07-17

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