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2Q1Y

Crystal Structure of cell division protein FtsZ from Mycobacterium tuberculosis in complex with GTP-gamma-S

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000917biological_processdivision septum assembly
A0000921biological_processseptin ring assembly
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0032153cellular_componentcell division site
A0043093biological_processFtsZ-dependent cytokinesis
A0045787biological_processpositive regulation of cell cycle
A0051258biological_processprotein polymerization
A0051301biological_processcell division
A0090529biological_processcell septum assembly
B0000287molecular_functionmagnesium ion binding
B0000917biological_processdivision septum assembly
B0000921biological_processseptin ring assembly
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0032153cellular_componentcell division site
B0043093biological_processFtsZ-dependent cytokinesis
B0045787biological_processpositive regulation of cell cycle
B0051258biological_processprotein polymerization
B0051301biological_processcell division
B0090529biological_processcell septum assembly
Functional Information from PDB Data
site_idAC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE GSP A 401
ChainResidue
AGLY17
AGLY101
AGLY104
AGLY105
ATHR106
AGLY107
APRO132
AGLU136
AARG140
APHE180
AALA183
AGLY18
AASP184
AHOH402
AHOH404
AHOH415
AHOH420
AHOH429
AHOH434
AHOH443
AHOH446
AGLY19
AASN22
ATHR42
AGLY67
AALA68
AGLY69
AALA70

Functional Information from PROSITE/UniProt
site_idPS01134
Number of Residues35
DetailsFTSZ_1 FtsZ protein signature 1. NTDaQaLlmsdadvkldvgrdstr.GlGAGAdPevG
ChainResidueDetails
AASN41-GLY75

site_idPS01135
Number of Residues22
DetailsFTSZ_2 FtsZ protein signature 2. DMvFVTAGeGGGTGTGGAPVVA
ChainResidueDetails
AASP94-ALA115

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:15342249, ECO:0000269|PubMed:23888039
ChainResidueDetails
AGLY18
BASP184
AGLY105
AGLU136
AARG140
AASP184
BGLY18
BGLY105
BGLU136
BARG140

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PDB entries from 2024-10-16

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