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4IAP

Crystal structure of PH domain of Osh3 from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme 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
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 Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1401
ChainResidue
AARG1242
ATYR1255
AARG1265
AHOH1518

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1402
ChainResidue
ALYS1240
AARG1242

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1403
ChainResidue
ALYS1279
ALYS1280
AALA1277
AASN1278
ALYS1279

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1404
ChainResidue
ATHR1142
APRO1143
AASN1144
AARG1145
AHOH1534
AHOH1542

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1405
ChainResidue
AARG222
ATYR1250
AHOH1558
BARG1076

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1401
ChainResidue
BARG1242
BTYR1255
BARG1265
BHOH1509

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1402
ChainResidue
BLYS1240
BARG1242

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1403
ChainResidue
BTHR1142
BPRO1143
BASN1144
BARG1145
BHOH1521

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
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
AGLU1011
BGLU1011

site_idSWS_FT_FI2
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
AASN1020
BASN1020

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104
BLEU1032
BPHE1104

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1117
AASN1132
BSER1117
BASN1132

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1011proton shuttle (general acid/base)
AASN1020covalent catalysis

site_idMCSA2
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
BGLU1011proton shuttle (general acid/base)
BASN1020covalent catalysis

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PDB entries from 2024-08-28

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