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8AYH

Structure of Complement C5 in Complex with small molecule inhibitor and CVF

Replaces:  6I2X
Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006954biological_processinflammatory response
A0006956biological_processcomplement activation
B0004866molecular_functionendopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006954biological_processinflammatory response
B0006956biological_processcomplement activation
C0004866molecular_functionendopeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DDNEDGFIAdsDI
ChainResidueDetails
BASP733-ILE745

site_idPS00477
Number of Residues9
DetailsALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PsGCGEQnM
ChainResidueDetails
BPRO990-MET998

site_idPS01177
Number of Residues35
DetailsANAPHYLATOXIN_1 Anaphylatoxin domain signature. CCydGacvnnde.TCEqraarisl.GprCikafte.CC
ChainResidueDetails
ACYS698-CYS732

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BPRO516
BASP539
BVAL540
BASP542

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN153
BASN158

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:21217642
ChainResidueDetails
BASN209
BASN1346

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Isoglutamyl cysteine thioester (Cys-Gln) => ECO:0000250
ChainResidueDetails
BCYS993
BGLN996

222624

PDB entries from 2024-07-17

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