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6A73

Complex structure of CSN2 with IP6

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 Residues7
Detailsbinding site for residue IHP A 401
ChainResidue
ALYS40
ALYS43
ALYS73
AGLN74
ALYS77
ATYR107
ASER114

site_idAC2
Number of Residues9
Detailsbinding site for residue SO4 A 402
ChainResidue
AASN305
AARG306
AHOH516
AHOH519
BSER199
BLEU200
BASN201
ATHR303
APRO304

site_idAC3
Number of Residues7
Detailsbinding site for residue IHP B 401
ChainResidue
BLYS40
BLYS43
BLYS70
BLYS73
BGLN74
BLYS77
BTYR107

site_idAC4
Number of Residues10
Detailsbinding site for residue SO4 B 402
ChainResidue
ASER199
ALEU200
AASN201
BTHR303
BPRO304
BASN305
BARG306
BHOH521
BHOH530
BHOH531

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
AGLU172
BGLU172

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
AASP181
BASP181

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU193
APHE265
BLEU193
BPHE265

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER278
AASN293
BSER278
BASN293

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU172proton shuttle (general acid/base)
AASP181covalent catalysis

site_idMCSA2
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
BGLU172proton shuttle (general acid/base)
BASP181covalent catalysis

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PDB entries from 2024-06-12

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