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1T8Y

Crystal Structure of E.coli AMP Nucleosidase complexed with phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0008714molecular_functionAMP nucleosidase activity
A0009116biological_processnucleoside metabolic process
A0016787molecular_functionhydrolase activity
A0044209biological_processAMP salvage
A0046033biological_processAMP metabolic process
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0008714molecular_functionAMP nucleosidase activity
B0009116biological_processnucleoside metabolic process
B0016787molecular_functionhydrolase activity
B0044209biological_processAMP salvage
B0046033biological_processAMP metabolic process
C0003824molecular_functioncatalytic activity
C0005829cellular_componentcytosol
C0008714molecular_functionAMP nucleosidase activity
C0009116biological_processnucleoside metabolic process
C0016787molecular_functionhydrolase activity
C0044209biological_processAMP salvage
C0046033biological_processAMP metabolic process
D0003824molecular_functioncatalytic activity
D0005829cellular_componentcytosol
D0008714molecular_functionAMP nucleosidase activity
D0009116biological_processnucleoside metabolic process
D0016787molecular_functionhydrolase activity
D0044209biological_processAMP salvage
D0046033biological_processAMP metabolic process
E0003824molecular_functioncatalytic activity
E0005829cellular_componentcytosol
E0008714molecular_functionAMP nucleosidase activity
E0009116biological_processnucleoside metabolic process
E0016787molecular_functionhydrolase activity
E0044209biological_processAMP salvage
E0046033biological_processAMP metabolic process
F0003824molecular_functioncatalytic activity
F0005829cellular_componentcytosol
F0008714molecular_functionAMP nucleosidase activity
F0009116biological_processnucleoside metabolic process
F0016787molecular_functionhydrolase activity
F0044209biological_processAMP salvage
F0046033biological_processAMP metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 F 501
ChainResidue
ALYS367
ATHR372
FSER472
FARG473
FLYS474

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 C 502
ChainResidue
CARG473
CLYS474
BLYS367
BLEU370
BARG371
BTHR372

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 503
ChainResidue
BSER472
BARG473
BLYS474
CLYS367
CARG371
CTHR372

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 E 504
ChainResidue
DLYS367
DARG371
DTHR372
ESER472
EARG473
ELYS474

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 D 505
ChainResidue
DSER472
DARG473
DLYS474
ELYS367
ELEU370
EARG371
ETHR372

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 506
ChainResidue
AARG473
ALYS474
FLYS367
FARG371
FTHR372

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PDB entries from 2024-06-12

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