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2FMI

Crystal structure of CheY in complex with CheZ 200-214 solved from a F432 crystal grown in Tris (pH 8.4)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000160biological_processphosphorelay signal transduction system
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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 150
ChainResidue
ALYS70
ALYS70
ALYS70
AHOH220
AHOH220
AHOH220

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRS A 151
ChainResidue
AGOL152
AGOL152
AGOL152
AHOH167
AHOH167
AALA74
AALA74
AALA74

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 152
ChainResidue
AARG73
AARG73
AALA74
AASP75
ASER79
ASER79
ATRS151
ATRS151
ATRS151

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9
ChainResidueDetails
AASP13

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16674976, ECO:0000269|PubMed:18083806, ECO:0000269|PubMed:8257674, ECO:0007744|PDB:2CHE, ECO:0007744|PDB:2FKA, ECO:0007744|PDB:2FLW, ECO:0007744|PDB:2FMH, ECO:0007744|PDB:2FMK, ECO:0007744|PDB:2PL9, ECO:0007744|PDB:2PMC
ChainResidueDetails
APHE14
ATRP58
AMET60

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1902474, ECO:0000269|PubMed:3280143
ChainResidueDetails
ATRP58

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250
ChainResidueDetails
AGLU93
APRO110

237735

PDB entries from 2025-06-18

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