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3N1P

Crystal Structure of IhhN bound to BOCFn3

Functional Information from GO Data
ChainGOidnamespacecontents
B0007267biological_processcell-cell signaling
B0007275biological_processmulticellular organism development
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 194
ChainResidue
BHIS145
BASP152
BGLU181
BHIS187

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 195
ChainResidue
BGLU94
BGLU95
BASP100
BTHR130
BGLU131

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 196
ChainResidue
BHOH2
BGLU95
BGLU131
BASP134
BASP136
CHOH1

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20519495","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20519495","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21537345","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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