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2OBL

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
AHOH1297
AHOH1297

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 1201
ChainResidue
AARG273
AARG276
AHOH1396

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IMD A 1295
ChainResidue
ALEU203
AILE204
AGLU206
AVAL211
AASP266
AHOH1319

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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