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1G0T

DSBC MUTANT C101S

Functional Information from GO Data
ChainGOidnamespacecontents
A0003756molecular_functionprotein disulfide isomerase activity
A0015035molecular_functionprotein-disulfide reductase activity
A0015036molecular_functiondisulfide oxidoreductase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0042803molecular_functionprotein homodimerization activity
A0046688biological_processresponse to copper ion
A0061077biological_processchaperone-mediated protein folding
B0003756molecular_functionprotein disulfide isomerase activity
B0015035molecular_functionprotein-disulfide reductase activity
B0015036molecular_functiondisulfide oxidoreductase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0042803molecular_functionprotein homodimerization activity
B0046688biological_processresponse to copper ion
B0061077biological_processchaperone-mediated protein folding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 501
ChainResidue
AGLY181
ATHR182
AGLY195
ATYR196

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 512
ChainResidueDetails
AASP95increase nucleophilicity, proton acceptor, proton donor
ACYS98electrofuge, electrophile, nucleofuge, nucleophile, proton acceptor, proton donor
ASER101nucleophile, proton donor
AARG125increase nucleophilicity

site_idMCSA2
Number of Residues4
DetailsM-CSA 512
ChainResidueDetails
BASP95increase nucleophilicity, proton acceptor, proton donor
BCYS98electrofuge, electrophile, nucleofuge, nucleophile, proton acceptor, proton donor
BSER101nucleophile, proton donor
BARG125increase nucleophilicity

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PDB entries from 2024-05-29

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