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1NZI

Crystal Structure of the CUB1-EGF Interaction Domain of Complement Protease C1s

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
B0005509molecular_functioncalcium ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
AASP116
AILE117
AGLU119
AASN134
APHE135
AGLY138
AHOH1005

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 1002
ChainResidue
BGLU119
BASN134
BPHE135
BGLY138
BHOH1010
BASP116
BILE117

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1003
ChainResidue
AGLU45
AASP53
AASP98
AHOH1109
AHOH1110

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1004
ChainResidue
BGLU45
BASP53
BASP98
BHOH1122
BHOH1134

Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CnNfiggYfCsC
ChainResidueDetails
ACYS132-CYS143

site_idPS01187
Number of Residues26
DetailsEGF_CA Calcium-binding EGF-like domain signature. DiNECtdfvdvp.......Cshf....CnNfiggYfC
ChainResidueDetails
AASP116-CYS141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING:
ChainResidueDetails
AGLU45
BGLU45
BASP53
BASP98
BASP116
BILE117
BGLU119
BASN134
BPHE135
BGLY138
AASP53
AASP98
AASP116
AILE117
AGLU119
AASN134
APHE135
AGLY138

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: (3R)-3-hydroxyasparagine => ECO:0000269|PubMed:2141278
ChainResidueDetails
AASN134
BASN134

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2141278
ChainResidueDetails
AASN159
BASN159

218853

PDB entries from 2024-04-24

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