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5KLP

Crystal structure of HopZ1a in complex with IP6

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 Residues24
Detailsbinding site for residue IHP A 401
ChainResidue
AARG49
ASER314
AHIS317
AARG326
APHE355
AGLN358
AARG362
AHOH528
AHOH540
AHOH558
AHOH564
ALYS53
AHOH565
AHOH585
AHOH601
AHOH608
BHOH531
AARG106
AASN222
AILE225
ALYS226
ALYS229
ALYS289
AHIS290

site_idAC2
Number of Residues11
Detailsbinding site for residue CIT A 402
ChainResidue
AHIS150
AGLY176
AALA177
AARG178
ATYR179
AGLN180
AGLN181
AARG184
AHOH554
AHOH569
AHOH641

site_idAC3
Number of Residues6
Detailsbinding site for residue CIT A 403
ChainResidue
AALA93
AHIS114
APRO138
ALYS149
AHIS151
AHOH552

site_idAC4
Number of Residues22
Detailsbinding site for residue IHP B 401
ChainResidue
BARG49
BLYS53
BARG106
BASN222
BILE225
BLYS226
BLYS229
BLYS289
BHIS290
BSER314
BHIS317
BARG326
BPHE355
BGLN358
BARG362
BHOH501
BHOH509
BHOH515
BHOH542
BHOH552
BHOH563
BHOH585

site_idAC5
Number of Residues7
Detailsbinding site for residue CIT B 402
ChainResidue
BALA93
BTHR94
BHIS114
BPRO138
BLYS149
BHIS151
BHOH572

site_idAC6
Number of Residues8
Detailsbinding site for residue CIT B 403
ChainResidue
BHIS150
BGLY176
BALA177
BARG178
BTYR179
BGLN180
BGLN181
BARG184

site_idAC7
Number of Residues25
Detailsbinding site for residue IHP C 401
ChainResidue
CHOH549
CHOH561
CHOH576
CHOH594
CARG49
CLYS53
CARG106
CASN222
CILE225
CLYS226
CLYS229
CLYS289
CHIS290
CSER314
CHIS317
CARG326
CPHE355
CGLN358
CARG362
CHOH502
CHOH504
CHOH514
CHOH517
CHOH528
CHOH542

site_idAC8
Number of Residues11
Detailsbinding site for residue CIT C 402
ChainResidue
CHIS150
CGLY176
CALA177
CARG178
CTYR179
CGLN180
CGLN181
CARG184
CHOH516
CHOH544
CHOH553

site_idAC9
Number of Residues9
Detailsbinding site for residue CIT C 403
ChainResidue
CALA93
CTHR94
CHIS114
CARG116
CPRO138
CLYS149
CHIS151
CHOH510
CHOH531

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

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

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

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

site_idSWS_FT_FI5
Number of Residues18
DetailsBINDING: BINDING => ECO:0007744|PDB:5KLQ
ChainResidueDetails
AALA292
AARG331
ASER344
BHIS150
BALA177
BALA211
BALA292
BARG331
BSER344
CHIS150
CALA177
CALA211
CALA292
CARG331
CSER344
AHIS150
AALA177
AALA211

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

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PDB entries from 2024-06-12

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