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1XK6

Crystal Structure- P1 form- of Escherichia coli Crotonobetainyl-CoA: carnitine CoA Transferase (CaiB)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0008410molecular_functionCoA-transferase activity
A0008735molecular_functionL-carnitine CoA-transferase activity
A0009437biological_processcarnitine metabolic process
A0016740molecular_functiontransferase activity
A0016782molecular_functiontransferase activity, transferring sulphur-containing groups
A0042413biological_processcarnitine catabolic process
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0008410molecular_functionCoA-transferase activity
B0008735molecular_functionL-carnitine CoA-transferase activity
B0009437biological_processcarnitine metabolic process
B0016740molecular_functiontransferase activity
B0016782molecular_functiontransferase activity, transferring sulphur-containing groups
B0042413biological_processcarnitine catabolic process
C0003824molecular_functioncatalytic activity
C0005737cellular_componentcytoplasm
C0008410molecular_functionCoA-transferase activity
C0008735molecular_functionL-carnitine CoA-transferase activity
C0009437biological_processcarnitine metabolic process
C0016740molecular_functiontransferase activity
C0016782molecular_functiontransferase activity, transferring sulphur-containing groups
C0042413biological_processcarnitine catabolic process
D0003824molecular_functioncatalytic activity
D0005737cellular_componentcytoplasm
D0008410molecular_functionCoA-transferase activity
D0008735molecular_functionL-carnitine CoA-transferase activity
D0009437biological_processcarnitine metabolic process
D0016740molecular_functiontransferase activity
D0016782molecular_functiontransferase activity, transferring sulphur-containing groups
D0042413biological_processcarnitine catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01050, ECO:0000305|PubMed:15518548
ChainResidueDetails
AASP169
BASP169
CASP169
DASP169

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01050, ECO:0000269|PubMed:15518548
ChainResidueDetails
ALYS97
AARG104
BLYS97
BARG104
CLYS97
CARG104
DLYS97
DARG104

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xvt
ChainResidueDetails
AASP169

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xvt
ChainResidueDetails
BASP169

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xvt
ChainResidueDetails
CASP169

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xvt
ChainResidueDetails
DASP169

site_idMCSA1
Number of Residues1
DetailsM-CSA 531
ChainResidueDetails
AASP169covalently attached, electrofuge, electrophile, nucleofuge, nucleophile

site_idMCSA2
Number of Residues1
DetailsM-CSA 531
ChainResidueDetails
BASP169covalently attached, electrofuge, electrophile, nucleofuge, nucleophile

site_idMCSA3
Number of Residues1
DetailsM-CSA 531
ChainResidueDetails
CASP169covalently attached, electrofuge, electrophile, nucleofuge, nucleophile

site_idMCSA4
Number of Residues1
DetailsM-CSA 531
ChainResidueDetails
DASP169covalently attached, electrofuge, electrophile, nucleofuge, nucleophile

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PDB entries from 2024-07-17

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