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2ODQ

Complement component C2a, the catalytic fragment of C3- and C5-convertase of human complement

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU483-CYS488

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SPckGESGGAVF
ChainResidueDetails
ASER653-PHE664

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:17027507
ChainResidueDetails
AHIS487
AASP541
ASER659

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ASER242
ASER244
ATHR317

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN270

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17027507, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN313

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17027507
ChainResidueDetails
AASN447
AASN601

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN451

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN631

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP541
AHIS487

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER659
AGLY660

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY657
ASER659

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER659
AASP541
AHIS487

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER659
AASP541
AHIS487
AGLY660

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY657
ASER659
AASP541
AHIS487

site_idMCSA1
Number of Residues3
DetailsM-CSA 688
ChainResidueDetails
AHIS487proton acceptor, proton donor
AASP541electrostatic stabiliser
ASER659electrostatic stabiliser

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PDB entries from 2025-06-18

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