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2HTB

Crystal Structure of a putative mutarotase (YeaD) from Salmonella typhimurium in monoclinic form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0016853molecular_functionisomerase activity
A0030246molecular_functioncarbohydrate binding
A0047938molecular_functionglucose-6-phosphate 1-epimerase activity
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0016853molecular_functionisomerase activity
B0030246molecular_functioncarbohydrate binding
B0047938molecular_functionglucose-6-phosphate 1-epimerase activity
C0003824molecular_functioncatalytic activity
C0005737cellular_componentcytoplasm
C0005975biological_processcarbohydrate metabolic process
C0016853molecular_functionisomerase activity
C0030246molecular_functioncarbohydrate binding
C0047938molecular_functionglucose-6-phosphate 1-epimerase activity
D0003824molecular_functioncatalytic activity
D0005737cellular_componentcytoplasm
D0005975biological_processcarbohydrate metabolic process
D0016853molecular_functionisomerase activity
D0030246molecular_functioncarbohydrate binding
D0047938molecular_functionglucose-6-phosphate 1-epimerase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q03161, ECO:0000305|PubMed:17242513
ChainResidueDetails
AHIS164
AGLU267
BHIS164
BGLU267
CHIS164
CGLU267
DHIS164
DGLU267

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q03161
ChainResidueDetails
AARG74
AARG99
AASP208
BARG74
BARG99
BASP208
CARG74
CARG99
CASP208
DARG74
DARG99
DASP208

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PDB entries from 2024-06-12

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