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3MM0

Crystal structure of chimeric avidin

Functional Information from GO Data
ChainGOidnamespacecontents
A0009374molecular_functionbiotin binding
B0009374molecular_functionbiotin binding
C0009374molecular_functionbiotin binding
D0009374molecular_functionbiotin binding
E0009374molecular_functionbiotin binding
F0009374molecular_functionbiotin binding
G0009374molecular_functionbiotin binding
H0009374molecular_functionbiotin binding
I0009374molecular_functionbiotin binding
K0009374molecular_functionbiotin binding
M0009374molecular_functionbiotin binding
N0009374molecular_functionbiotin binding
Functional Information from PROSITE/UniProt
site_idPS00577
Number of Residues15
DetailsAVIDIN_1 Avidin-like domain signature. DdwKAtrVGyNiFTR
ChainResidueDetails
AASP108-ARG122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues84
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15858262","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Y52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y55","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000230","evidences":[{"source":"PubMed","id":"5100763","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues23
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15858262","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Y52","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

245011

PDB entries from 2025-11-19

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