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3Q9L

The structure of the dimeric E.coli MinD-ATP complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000917biological_processdivision septum assembly
A0000918biological_processdivision septum site selection
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0007059biological_processchromosome segregation
A0008298biological_processintracellular mRNA localization
A0009898cellular_componentcytoplasmic side of plasma membrane
A0016887molecular_functionATP hydrolysis activity
A0042802molecular_functionidentical protein binding
A0051301biological_processcell division
A0051782biological_processnegative regulation of cell division
A0060187cellular_componentcell pole
B0000917biological_processdivision septum assembly
B0000918biological_processdivision septum site selection
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0007059biological_processchromosome segregation
B0008298biological_processintracellular mRNA localization
B0009898cellular_componentcytoplasmic side of plasma membrane
B0016887molecular_functionATP hydrolysis activity
B0042802molecular_functionidentical protein binding
B0051301biological_processcell division
B0051782biological_processnegative regulation of cell division
B0060187cellular_componentcell pole
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 700
ChainResidue
ATHR17
AHOH261
AHOH262
AHOH263
AATP800

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ATP A 800
ChainResidue
ALYS16
ATHR17
ATHR18
AALA123
AARG182
APRO212
AGLU213
AASP214
AVAL217
AHOH262
AHOH263
AHOH293
AHOH305
AHOH310
AMG700
BLYS11
BGLY12
BGLU146
AGLY12
AGLY13
AVAL14
AGLY15

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 700
ChainResidue
BTHR17
BHOH261
BHOH262
BHOH263
BATP800

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ATP B 800
ChainResidue
ALYS11
AGLY12
AGLU146
BGLY12
BGLY13
BVAL14
BGLY15
BLYS16
BTHR17
BTHR18
BALA123
BARG182
BILE211
BPRO212
BGLU213
BASP214
BVAL217
BHOH261
BHOH263
BHOH287
BHOH301
BHOH312
BMG700

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q72H90
ChainResidueDetails
ALYS11
BLYS11

226707

PDB entries from 2024-10-30

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