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4BIU

Crystal structure of CpxAHDC (orthorhombic form 1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000155molecular_functionphosphorelay sensor kinase activity
A0007165biological_processsignal transduction
A0016020cellular_componentmembrane
A0016310biological_processphosphorylation
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0000155molecular_functionphosphorelay sensor kinase activity
B0007165biological_processsignal transduction
B0016020cellular_componentmembrane
B0016310biological_processphosphorylation
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
C0000155molecular_functionphosphorelay sensor kinase activity
C0007165biological_processsignal transduction
C0016020cellular_componentmembrane
C0016310biological_processphosphorylation
C0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
D0000155molecular_functionphosphorelay sensor kinase activity
D0007165biological_processsignal transduction
D0016020cellular_componentmembrane
D0016310biological_processphosphorylation
D0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
E0000155molecular_functionphosphorelay sensor kinase activity
E0007165biological_processsignal transduction
E0016020cellular_componentmembrane
E0016310biological_processphosphorylation
E0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
F0000155molecular_functionphosphorelay sensor kinase activity
F0007165biological_processsignal transduction
F0016020cellular_componentmembrane
F0016310biological_processphosphorylation
F0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ADP C 501
ChainResidue
CASN360
CLEU445
CARG363
CTYR364
CASP386
CPRO389
CVAL391
CILE399
CGLY420
CLEU421

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ADP E 501
ChainResidue
EASN360
EARG363
ETYR364
EASP386
EPRO389
EVAL391
EILE399
ETYR404
EGLY418
ELEU419
ELEU445

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADP F 501
ChainResidue
FASN360
FARG363
FTYR364
FASP386
FPRO389
FVAL391
FILE399
FARG405
FTHR406
FALA409
FTHR417
FGLY420
FLEU421
FLEU445

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 F 1455
ChainResidue
CPRO340
CTRP341
FGLY339
FPRO340
FTRP341

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 1456
ChainResidue
DGLY339
DPRO340
DTRP341
EGLY339
EPRO340
ETRP341

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 1457
ChainResidue
DASN360
DARG363
DTYR364
DGLY418

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"24492262","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues73
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24492262","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsModified residue: {"description":"Phosphohistidine; by autocatalysis","evidences":[{"source":"PROSITE-ProRule","id":"PRU00107","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24492262","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9401031","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues210
DetailsDomain: {"description":"Histidine kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00107","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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