Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4BIW

Crystal structure of CpxAHDC (hexagonal form)

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
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ANP A 501
ChainResidue
AASN360
AARG405
ATHR406
AALA409
AGLY416
AGLY418
ALEU419
AGLY420
ALEU421
ALEU445
AMG502
AARG363
AHOH2012
ATYR364
AASP386
APRO389
AGLY390
AVAL391
AILE399
ATYR404

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AASN360
AARG363
AANP501

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1456
ChainResidue
ALYS377
BARG446

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1457
ChainResidue
APRO441
AARG446
BLYS377

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ANP B 501
ChainResidue
AHIS248
AARG251
BASN360
BTYR364
BASP386
BPRO389
BVAL391
BILE399
BTYR404
BARG405
BTHR406
BALA409
BTHR417
BGLY418
BLEU419
BGLY420
BLEU421
BLEU445
BMG502

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 502
ChainResidue
BASN356
BASN360
BANP501

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:24492262
ChainResidueDetails
AHIS248
BHIS248

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:24492262
ChainResidueDetails
AHIS248
BGLY416
AARG359
AASP386
AARG405
AGLY416
BHIS248
BARG359
BASP386
BARG405

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphohistidine; by autocatalysis => ECO:0000255|PROSITE-ProRule:PRU00107, ECO:0000305|PubMed:24492262, ECO:0000305|PubMed:9401031
ChainResidueDetails
AHIS248
BHIS248

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon