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2BTO

Structure of BtubA from Prosthecobacter dejongeii

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005874cellular_componentmicrotubule
A0007010biological_processcytoskeleton organization
A0007017biological_processmicrotubule-based process
A0016787molecular_functionhydrolase activity
B0000166molecular_functionnucleotide binding
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005874cellular_componentmicrotubule
B0007010biological_processcytoskeleton organization
B0007017biological_processmicrotubule-based process
B0016787molecular_functionhydrolase activity
T0005515molecular_functionprotein binding
T0005737cellular_componentcytoplasm
T0005829cellular_componentcytosol
T0015035molecular_functionprotein-disulfide reductase activity
T0015036molecular_functiondisulfide oxidoreductase activity
T0030337molecular_functionDNA polymerase processivity factor activity
T0045454biological_processcell redox homeostasis
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE GTP A1433
ChainResidue
AGLY12
ATHR147
AGLY148
AVAL173
APRO175
AGLU185
AASN208
AVAL226
AASN230
AILE233
AHOH2102
AGLN13
AHOH2103
AHOH2104
AHOH2105
AHOH2106
AHOH2107
AHOH2108
TARG92
AALA14
AGLN17
AALA101
AGLY103
AALA142
AGLY145
AGLY146

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GTP B1433
ChainResidue
BGLY12
BGLN13
BALA14
BGLN17
BGLY100
BALA101
BGLY103
BALA142
BGLY145
BGLY146
BTHR147
BGLY148
BPRO175
BGLU185
BASN208
BVAL226
BASN230
BHOH2039

Functional Information from PROSITE/UniProt
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. LVdFWaeWCGPCKmIapiL
ChainResidueDetails
TLEU43-LEU61

site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
AGLY144-GLY150

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
TGLY52
TLYS55

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Deprotonates C-terminal active site Cys
ChainResidueDetails
TPHE46

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Contributes to redox potential value
ChainResidueDetails
TPRO53
TCYS54

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
TTYR89

218853

PDB entries from 2024-04-24

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