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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 Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02112
ChainResidueDetails
ALEU310
BLEU310

site_idSWS_FT_FI2
Number of Residues4
DetailsCROSSLNK: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) => ECO:0000269|PubMed:20066036
ChainResidueDetails

222926

PDB entries from 2024-07-24

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