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3H1E

Crystal structure of Mg(2+) and BeH(3)(-)-bound CheY of Helicobacter pylori

Functional Information from GO Data
ChainGOidnamespacecontents
A0000160biological_processphosphorelay signal transduction system
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006935biological_processchemotaxis
A0046872molecular_functionmetal ion binding
A0097588biological_processarchaeal or bacterial-type flagellum-dependent cell motility
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 201
ChainResidue
AMET12
AGLU30
ALYS105
AHOH171

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
ABEF301
AASP8
AASP53
AASN55
AHOH156
AHOH168

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BEF A 301
ChainResidue
ALYS17
AASP53
ATRP54
AASN55
ATHR83
ATHR84
ALYS105
AHOH168
AMG202

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
ALYS2
AASP46
ALYS48
AGLY87
ALYS88
AASN100
AHOH164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9
ChainResidueDetails
AASP7

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0007744|PDB:3GWG, ECO:0007744|PDB:3H1E, ECO:0007744|PDB:3H1G
ChainResidueDetails
AASP8
AASP53
AASN55

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:16207913
ChainResidueDetails
AASP53

218853

PDB entries from 2024-04-24

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