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4QPK

1.7 Angstrom Structure of a Bacterial Phosphotransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000160biological_processphosphorelay signal transduction system
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0018197biological_processpeptidyl-aspartic acid modification
A0042803molecular_functionprotein homodimerization activity
B0000160biological_processphosphorelay signal transduction system
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0018197biological_processpeptidyl-aspartic acid modification
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
AASP23
AARG61
APHE64
AALA65
APHE69
ATYR91
AHOH639

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
APRO158
AHIS177
AGLN180
AHOH447
AHOH623
AARG19
ALEU121

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 301
ChainResidue
BALA60
BGLU90
BARG93
BASN94

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BARG19
BILE20
BASP23
BARG61
BPHE64
BALA65
BPHE69
BTYR91

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 303
ChainResidue
AARG105
AHOH449
AHOH541
AHOH579
BALA75
BGLY76
BVAL77
BGLN78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"Phosphohistidine","evidences":[{"source":"PubMed","id":"26124143","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

250059

PDB entries from 2026-03-04

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