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8CML

Cryo-EM structure of complement C5 in complex with nanobodies UNbC5-1 and UNbC5-2

Functional Information from GO Data
ChainGOidnamespacecontents
B0004866molecular_functionendopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006954biological_processinflammatory response
B0006956biological_processcomplement activation
E0004866molecular_functionendopeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS01177
Number of Residues35
DetailsANAPHYLATOXIN_1 Anaphylatoxin domain signature. CCydGacvnnde.TCEqraarisl.GprCikafte.CC
ChainResidueDetails
BCYS698-CYS732

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:18536718, ECO:0007744|PDB:3CU7, ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9
ChainResidueDetails
BASN741

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:18536718, ECO:0000269|PubMed:21217642, ECO:0007744|PDB:3CU7, ECO:0007744|PDB:3KLS, ECO:0007744|PDB:3KM9
ChainResidueDetails
BASN911

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN1115

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
BASN1630

219869

PDB entries from 2024-05-15

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