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5XZ8

Crystal Structure of Phosphofructokinase from Staphylococcus aureus in complex with adenylylimidodiphosphate (the ATP analog) and fructose-6-phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003872molecular_function6-phosphofructokinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005945cellular_component6-phosphofructokinase complex
A0006002biological_processfructose 6-phosphate metabolic process
A0006096biological_processglycolytic process
A0008443molecular_functionphosphofructokinase activity
A0016208molecular_functionAMP binding
A0016301molecular_functionkinase activity
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0048029molecular_functionmonosaccharide binding
A0061621biological_processcanonical glycolysis
A0070095molecular_functionfructose-6-phosphate binding
Functional Information from PROSITE/UniProt
site_idPS00433
Number of Residues19
DetailsPHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvsvlGHvQRGGsptgaDR
ChainResidueDetails
AARG245-ARG263

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00339
ChainResidueDetails
AASP129

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339
ChainResidueDetails
AGLY11
AARG21
AASP103
AARG164
AARG245

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:29940104
ChainResidueDetails
AARG72
AGLY102

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:29940104
ChainResidueDetails
ATHR127
AMET171
AGLU224
AHIS251

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00339
ChainResidueDetails
AARG156
AGLY187
AARG213
ALYS215

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PDB entries from 2024-07-24

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