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2ZAG

Crystal structure of the SeMet-substituted soluble domain of STT3 from P. furiosus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004576molecular_functionoligosaccharyl transferase activity
A0006486biological_processprotein glycosylation
A0016020cellular_componentmembrane
B0004576molecular_functionoligosaccharyl transferase activity
B0006486biological_processprotein glycosylation
B0016020cellular_componentmembrane
C0004576molecular_functionoligosaccharyl transferase activity
C0006486biological_processprotein glycosylation
C0016020cellular_componentmembrane
D0004576molecular_functionoligosaccharyl transferase activity
D0006486biological_processprotein glycosylation
D0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 1
ChainResidue
AGLU554
AALA759
ATYR793
AGLU796

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 2
ChainResidue
BGLU554
BALA759
BTYR793
BGLU796

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 3
ChainResidue
CALA759
CTYR793
CGLU796
CGLU554

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA D 4
ChainResidue
DGLU554
DALA759
DTYR793
DGLU796

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 5
ChainResidue
AARG762
AARG866

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 6
ChainResidue
BARG762
BARG866

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 7
ChainResidue
CARG762
CPRO820
CARG866
CPHE895

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL D 8
ChainResidue
DARG762
DARG866
DPHE895

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1968
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AALA475-HIS967
BALA475-HIS967
CALA475-HIS967
DALA475-HIS967

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:B9KDD4
ChainResidueDetails
ATYR516
BTYR516
CTYR516
DTYR516

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Interacts with target acceptor peptide in protein substrate => ECO:0000250|UniProtKB:O29867
ChainResidueDetails
ALYS574
BLYS574
CLYS574
DLYS574

226707

PDB entries from 2024-10-30

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