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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
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:24492262
ChainResidueDetails
AHIS248
BHIS248
CHIS248
DHIS248
EHIS248
FHIS248

site_idSWS_FT_FI2
Number of Residues30
DetailsBINDING: BINDING => ECO:0000269|PubMed:24492262
ChainResidueDetails
AHIS248
BGLY416
CHIS248
CARG359
CASP386
CARG405
CGLY416
DHIS248
DARG359
DASP386
DARG405
AARG359
DGLY416
EHIS248
EARG359
EASP386
EARG405
EGLY416
FHIS248
FARG359
FASP386
FARG405
AASP386
FGLY416
AARG405
AGLY416
BHIS248
BARG359
BASP386
BARG405

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphohistidine; by autocatalysis => ECO:0000255|PROSITE-ProRule:PRU00107, ECO:0000305|PubMed:24492262, ECO:0000305|PubMed:9401031
ChainResidueDetails
AHIS248
BHIS248
CHIS248
DHIS248
EHIS248
FHIS248

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PDB entries from 2024-04-24

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