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5FCR

MOUSE COMPLEMENT FACTOR D

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0006957biological_processcomplement activation, alternative pathway
A0007219biological_processNotch signaling pathway
A0008236molecular_functionserine-type peptidase activity
A0009617biological_processresponse to bacterium
B0004175molecular_functionendopeptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006508biological_processproteolysis
B0006957biological_processcomplement activation, alternative pathway
B0007219biological_processNotch signaling pathway
B0008236molecular_functionserine-type peptidase activity
B0009617biological_processresponse to bacterium
C0004175molecular_functionendopeptidase activity
C0004252molecular_functionserine-type endopeptidase activity
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0006508biological_processproteolysis
C0006957biological_processcomplement activation, alternative pathway
C0007219biological_processNotch signaling pathway
C0008236molecular_functionserine-type peptidase activity
C0009617biological_processresponse to bacterium
D0004175molecular_functionendopeptidase activity
D0004252molecular_functionserine-type endopeptidase activity
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0006508biological_processproteolysis
D0006957biological_processcomplement activation, alternative pathway
D0007219biological_processNotch signaling pathway
D0008236molecular_functionserine-type peptidase activity
D0009617biological_processresponse to bacterium
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue EPE B 301
ChainResidue
BHIS91
BGLU100
BASP101
BASN179
BSER233
BTYR234
BMET236
BTRP237
BHOH545

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL B 302
ChainResidue
BGLU21
BARG150
BPRO152
BASP153
BVAL154
BHIS156

site_idAC3
Number of Residues10
Detailsbinding site for residue EPE C 301
ChainResidue
CHIS91
CGLU100
CASP101
CASN179
CSER233
CTYR234
CMET236
CTRP237
CHOH432
CHOH515

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 C 302
ChainResidue
CARG150
CPRO152
CASP153
CVAL154
CHIS156

site_idAC5
Number of Residues6
Detailsbinding site for residue DMS D 301
ChainResidue
DHIS91
DTYR234
DMET236
DTRP237
DHOH493
DHOH556

site_idAC6
Number of Residues6
Detailsbinding site for residue DMS D 302
ChainResidue
DGLU21
DARG150
DPRO152
DASP153
DVAL154
DHIS156

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LSAAHC
ChainResidueDetails
ALEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DTcrGDSGSPLV
ChainResidueDetails
AASP189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS57
DHIS57
DASP102
DSER195
AASP102
ASER195
BHIS57
BASP102
BSER195
CHIS57
CASP102
CSER195

site_idSWS_FT_FI2
Number of Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN36
DASN36
DASN240
DASN245
AASN240
AASN245
BASN36
BASN240
BASN245
CASN36
CASN240
CASN245

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16944957
ChainResidueDetails
AASN111
BASN111
CASN111
DASN111

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17330941
ChainResidueDetails
AASN164
BASN164
CASN164
DASN164

222415

PDB entries from 2024-07-10

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