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2XW9

Crystal Structure of Complement Factor D mutant S183A

Functional Information from GO Data
ChainGOidnamespacecontents
A0002376biological_processimmune system process
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0006956biological_processcomplement activation
A0006957biological_processcomplement activation, alternative pathway
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0009617biological_processresponse to bacterium
A0016787molecular_functionhydrolase activity
A0031093cellular_componentplatelet alpha granule lumen
A0031638biological_processzymogen activation
A0034774cellular_componentsecretory granule lumen
A0045087biological_processinnate immune response
A0051604biological_processprotein maturation
A0070062cellular_componentextracellular exosome
A1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1230
ChainResidue
AASP116
AVAL117
AVAL148
ALEU149
AASP150
AARG151
AMET169
ACYS170
AHOH2298

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 1231
ChainResidue
ASER178
ACYS179
AVAL197
ATHR198
AGLY200
AARG202
AGOL1232
AHOH2266
AHOH2269
AHOH2299
AHOH2300

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1232
ChainResidue
ALYS180
ASER201
AARG202
ACYS204
AGOL1231

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1233
ChainResidue
AHIS159
AGLU172
AARG207
AHOH2301

site_idCAT
Number of Residues3
DetailsCATALYTIC SITE SHOWS FLIPPED HIS 41 DUE TO SELF-INHIBITORY LOOP
ChainResidue
AHIS41
AASP89
ASER199

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LSAAHC
ChainResidueDetails
ALEU37-CYS42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues227
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsRegion: {"description":"Self-inhibitor loop","evidences":[{"source":"PubMed","id":"10022823","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9753554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"7592653","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9753554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"7592653","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"7592653","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21205667","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22362762","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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