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2OBM

Structural and biochemical analysis of a prototypical ATPase from the type III secretion system of pathogenic bacteria

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0009058biological_processbiosynthetic process
A0016887molecular_functionATP hydrolysis activity
A0030254biological_processprotein secretion by the type III secretion system
A0030257cellular_componenttype III protein secretion system complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
AASN328
AASN328
AASP333
AASP333
AHOH1003
AHOH1003

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADP A 600
ChainResidue
ASER184
ATHR185
AMET189
ALEU238
APHE355
AGLN426
ASER427
ATHR428
AHOH1037
AHOH1092
AHOH1107
AGLY180
AGLY182
ALYS183

Functional Information from PROSITE/UniProt
site_idPS00152
Number of Residues10
DetailsATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAIDIGLSAS
ChainResidueDetails
APRO356-SER365

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
AARG366

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
AARG207
ALYS183
AGLU206

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PDB entries from 2025-06-18

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