Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5KWA

complete structure of the Mycobacterium tuberculosis proteasomal ATPase Mpa

Functional Information from GO Data
ChainGOidnamespacecontents
A0000502cellular_componentproteasome complex
A0005524molecular_functionATP binding
A0010498biological_processproteasomal protein catabolic process
A0016887molecular_functionATP hydrolysis activity
A0019941biological_processmodification-dependent protein catabolic process
B0000502cellular_componentproteasome complex
B0005524molecular_functionATP binding
B0010498biological_processproteasomal protein catabolic process
B0016887molecular_functionATP hydrolysis activity
B0019941biological_processmodification-dependent protein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue ADP A 701
ChainResidue
AGLY255
AGLY516
AALA517
AGLN520
AMG702
AHOH806
APRO295
AGLY296
ACYS297
AGLY298
ALYS299
ATHR300
ALEU301
ATYR452

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 702
ChainResidue
ATHR300
AADP701
AHOH808

site_idAC3
Number of Residues16
Detailsbinding site for residue ADP B 701
ChainResidue
AARG427
BASP253
BGLY255
BPRO295
BGLY296
BCYS297
BGLY298
BLYS299
BTHR300
BLEU301
BTYR452
BGLY516
BALA517
BGLN520
BMG702
BHOH801

site_idAC4
Number of Residues4
Detailsbinding site for residue MG B 702
ChainResidue
AARG427
BTHR300
BADP701
BHOH801

Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues19
DetailsAAA AAA-protein family signature. ViVIgASNredmIDpAIl.R
ChainResidueDetails
AVAL409-ARG427

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02112","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

250059

PDB entries from 2026-03-04

PDB statisticsPDBj update infoContact PDBjnumon