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

1OJY

Decay accelerating factor (cd55): the structure of an intact human complement regulator.

Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT A 1254
ChainResidue
APRO134
AILE154
APHE156
ASER170
ATRP181
AASP183
APRO184
ALEU185

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT B 1255
ChainResidue
BILE154
BPHE156
BSER170
BTRP181
BASP183
BPRO184
BLEU185
BPRO134

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 1254
ChainResidue
ATYR213
AARG214
CTYR213
CARG214
CTYR234
CTHR236
CVAL237
CASN238

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT C 1256
ChainResidue
CPRO134
CILE154
CPHE156
CSER170
CTRP181
CASP183
CPRO184
CLEU185

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 1257
ChainResidue
AARG138
CGLN215
CSER216

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 D 1255
ChainResidue
BTYR213
BARG214
DTYR213
DARG214
DTHR236
DVAL237
DASN238

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT D 1256
ChainResidue
DPRO134
DILE154
DPHE156
DSER170
DTRP181
DASP183
DPRO184
DLEU185

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1256
ChainResidue
BARG214
BGLN215
BSER216
DGLN141
DASN159
DTHR160
DHOH2024

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 1255
ChainResidue
AARG214
AGLN215
ASER216
CGLN141
CASN159
CTHR160

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 1258
ChainResidue
CPHE156
CSER157
CCYS158
CLEU164
CASP240

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 1257
ChainResidue
DPHE156
DSER157
DCYS158
DLYS163
DLEU164
DASP240

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 1258
ChainResidue
DPRO7
DASP9
DVAL10
DALA13
DGLN14
DPRO15

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL D 1259
ChainResidue
AARG252
BARG138
DGLN215
DSER216

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues244
DetailsDomain: {"description":"Sushi 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues256
DetailsDomain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues244
DetailsDomain: {"description":"Sushi 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues248
DetailsDomain: {"description":"Sushi 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

251422

PDB entries from 2026-04-01

PDB statisticsPDBj update infoContact PDBjnumon