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1RD4

An allosteric inhibitor of LFA-1 bound to its I-domain

Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE L08 A 328
ChainResidue
APHE153
AGLU284
APHE285
AVAL286
ALYS287
ALEU298
AGLU301
ALEU302
ALYS305
BVAL308
AVAL157
ATYR166
AVAL233
AILE235
AILE255
ATYR257
AILE258
AILE259

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE L08 B 1328
ChainResidue
AVAL308
BPHE153
BVAL157
BTYR166
BVAL233
BILE235
BTYR257
BILE258
BILE259
BGLU284
BPHE285
BVAL286
BLYS287
BLEU298
BGLU301
BLEU302
BLYS305

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE L08 C 2328
ChainResidue
CPHE134
CPHE153
CTYR166
CVAL233
CILE235
CILE255
CTYR257
CILE258
CILE259
CGLU284
CPHE285
CVAL286
CLYS287
CLEU298
CGLU301
CLEU302
DVAL308

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE L08 D 3328
ChainResidue
CVAL308
DPHE153
DVAL157
DTYR166
DVAL233
DILE235
DILE255
DTYR257
DILE258
DILE259
DGLU284
DPHE285
DVAL286
DLYS287
DLEU298
DGLU301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues684
DetailsDomain: {"description":"VWFA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00219","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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