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4WTV

Crystal structure of the phosphatidylinositol 4-kinase IIbeta

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004430molecular_function1-phosphatidylinositol 4-kinase activity
A0009253biological_processpeptidoglycan catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
B0003796molecular_functionlysozyme activity
B0004430molecular_function1-phosphatidylinositol 4-kinase activity
B0009253biological_processpeptidoglycan catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016998biological_processcell wall macromolecule catabolic process
B0030430cellular_componenthost cell cytoplasm
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0044659biological_processviral release from host cell by cytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue ATP A 1201
ChainResidue
ASER133
AHOH1322
AHOH1367
AHOH1426
AHOH1433
BTYR268
BARG271
BLYS272
AVAL146
ALYS148
AGLN257
ALEU258
APHE259
AVAL260
AILE343
AASP344

site_idAC2
Number of Residues18
Detailsbinding site for residue ATP B 1201
ChainResidue
AARG271
ALYS272
BSER131
BSER133
BPHE135
BVAL146
BLYS148
BGLN257
BLEU258
BPHE259
BVAL260
BILE343
BASP344
BHOH1349
BHOH1360
BHOH1399
BHOH1436
BHOH1446

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:26143926, ECO:0007744|PDB:4WTV
ChainResidueDetails
ASER133
BASP344
ALYS148
AGLN257
AARG271
AASP344
BSER133
BLYS148
BGLN257
BARG271

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU1010
BGLU1010

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP1019
BASP1019

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1031
APHE1103
BLEU1031
BPHE1103

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1116
AASN1131
BSER1116
BASN1131

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1010proton shuttle (general acid/base)
AASP1019covalent catalysis

site_idMCSA2
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
BGLU1010proton shuttle (general acid/base)
BASP1019covalent catalysis

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PDB entries from 2024-07-24

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