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2YOQ

Structure of FAM3B PANDER E30 construct

Functional Information from GO Data
ChainGOidnamespacecontents
A0005125molecular_functioncytokine activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005641cellular_componentnuclear envelope lumen
A0006915biological_processapoptotic process
A0007165biological_processsignal transduction
A0030073biological_processinsulin secretion
A0030246molecular_functioncarbohydrate binding
B0005125molecular_functioncytokine activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005641cellular_componentnuclear envelope lumen
B0006915biological_processapoptotic process
B0007165biological_processsignal transduction
B0030073biological_processinsulin secretion
B0030246molecular_functioncarbohydrate binding
C0005125molecular_functioncytokine activity
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005641cellular_componentnuclear envelope lumen
C0006915biological_processapoptotic process
C0007165biological_processsignal transduction
C0030073biological_processinsulin secretion
C0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1196
ChainResidue
AARG107
ATYR130
AASP157
AASP158
APHE184
AARG185

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1196
ChainResidue
BARG185
BHOH2065
BARG107
BTYR130
BASP157

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 1195
ChainResidue
CARG107
CTYR130
CASP157
CPHE184
CARG185
CHOH2126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN208
BASN208
CASN208

221716

PDB entries from 2024-06-26

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