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5KLQ

Crystal structure of HopZ1a in complex with IP6 and CoA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000822molecular_functioninositol hexakisphosphate binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0016020cellular_componentmembrane
A0016413molecular_functionO-acetyltransferase activity
A0016746molecular_functionacyltransferase activity
A0020002cellular_componenthost cell plasma membrane
A0030430cellular_componenthost cell cytoplasm
A0035821biological_processmodulation of process of another organism
A0042025cellular_componenthost cell nucleus
A0044163cellular_componenthost cytoskeleton
A0090729molecular_functiontoxin activity
B0000822molecular_functioninositol hexakisphosphate binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0016020cellular_componentmembrane
B0016413molecular_functionO-acetyltransferase activity
B0016746molecular_functionacyltransferase activity
B0020002cellular_componenthost cell plasma membrane
B0030430cellular_componenthost cell cytoplasm
B0035821biological_processmodulation of process of another organism
B0042025cellular_componenthost cell nucleus
B0044163cellular_componenthost cytoskeleton
B0090729molecular_functiontoxin activity
C0000822molecular_functioninositol hexakisphosphate binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0016020cellular_componentmembrane
C0016413molecular_functionO-acetyltransferase activity
C0016746molecular_functionacyltransferase activity
C0020002cellular_componenthost cell plasma membrane
C0030430cellular_componenthost cell cytoplasm
C0035821biological_processmodulation of process of another organism
C0042025cellular_componenthost cell nucleus
C0044163cellular_componenthost cytoskeleton
C0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue IHP C 401
ChainResidue
CLYS53
CHIS317
CARG326
CPHE355
CGLN358
CARG362
CARG106
CASN222
CILE225
CLYS226
CLYS229
CLYS289
CHIS290
CSER314

site_idAC2
Number of Residues15
Detailsbinding site for residue COA C 402
ChainResidue
CALA172
CVAL173
CGLY176
CALA177
CGLN181
CLYS211
CTHR212
CSER293
CLEU294
CTHR295
CARG331
CARG334
CASN345
CGLN347
CPHE348

site_idAC3
Number of Residues16
Detailsbinding site for residue IHP A 401
ChainResidue
AARG49
ALYS53
AARG106
AASN222
AILE225
ALYS226
ALYS229
ALYS289
AHIS290
AASN313
ASER314
AHIS317
AARG326
APHE355
AGLN358
AARG362

site_idAC4
Number of Residues13
Detailsbinding site for residue COA A 402
ChainResidue
AHIS150
AALA172
ALYS211
ATHR212
ASER213
ASER293
ALEU294
ATHR295
AARG331
AARG334
ASER344
AGLN347
APHE348

site_idAC5
Number of Residues13
Detailsbinding site for residue IHP B 401
ChainResidue
BLYS53
BARG106
BASN222
BLYS226
BLYS229
BLYS289
BASN313
BSER314
BHIS317
BARG326
BPHE355
BGLN358
BARG362

site_idAC6
Number of Residues11
Detailsbinding site for residue COA B 402
ChainResidue
BLYS211
BTHR212
BALA292
BSER293
BLEU294
BTHR295
BARG334
BARG335
BSER344
BGLN347
BPHE348

site_idAC7
Number of Residues4
Detailsbinding site for residue CIT B 403
ChainResidue
AARG62
AHIS63
BHIS150
BARG184

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:27525589
ChainResidueDetails
CHIS150
CGLU170
AHIS150
AGLU170
BHIS150
BGLU170

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:27525589, ECO:0000305|PubMed:22319451
ChainResidueDetails
CCYS216
ACYS216
BCYS216

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0007744|PDB:5KLP
ChainResidueDetails
CARG49
AARG49
BARG49

site_idSWS_FT_FI4
Number of Residues27
DetailsBINDING: BINDING => ECO:0007744|PDB:5KLP, ECO:0007744|PDB:5KLQ
ChainResidueDetails
CLYS53
ALYS53
AARG106
AASN222
ALYS226
ALYS289
ASER314
AARG326
AGLN358
AARG362
BLYS53
CARG106
BARG106
BASN222
BLYS226
BLYS289
BSER314
BARG326
BGLN358
BARG362
CASN222
CLYS226
CLYS289
CSER314
CARG326
CGLN358
CARG362

site_idSWS_FT_FI5
Number of Residues18
DetailsBINDING: BINDING => ECO:0007744|PDB:5KLQ
ChainResidueDetails
CHIS150
AALA292
AARG331
ASER344
BHIS150
BALA177
BLYS211
BALA292
BARG331
BSER344
CALA177
CLYS211
CALA292
CARG331
CSER344
AHIS150
AALA177
ALYS211

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:22319451, ECO:0000269|PubMed:26217317
ChainResidueDetails
CLYS289
ALYS289
BLYS289

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PDB entries from 2024-05-01

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