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1SWZ

Use of an ion-binding site to bypass the 1000-atom limit to ab initio structure determination by direct methods

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0008152biological_processmetabolic process
A0009253biological_processpeptidoglycan catabolic process
A0016787molecular_functionhydrolase activity
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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 168
ChainResidue
AARG76
AARG80
ALYS85
AASP89
AHOH1071
AHOH1078

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE RB A 601
ChainResidue
AHOH1006
AHOH1080
AHOH1211
AHOH1247
AASP89
ALEU91
AGLU96

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE RB A 602
ChainResidue
AGLU11
ATYR18
AHOH1121
AHOH1204
AHOH1212

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE RB A 603
ChainResidue
AGLY30
APHE104
AGLN105
AHOH1058
AHOH1122
AHOH1208

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE RB A 604
ChainResidue
ASER44
AGLY113
ATHR115
AHOH1282

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE RB A 605
ChainResidue
ATYR25
APRO37
AHOH1206
AHOH1207

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 611
ChainResidue
AARG125
ATRP126
AASP127
AGLU128
AHOH1063
AHOH1711

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL A 612
ChainResidue
ALYS124
ATHR142
APRO143
AASN144
AARG145
AHOH1004
AHOH1287

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 613
ChainResidue
AASN132
ALYS135
AHOH1034

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 614
ChainResidue
AHIS31
ALYS135
AHOH1017

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 599
ChainResidue
AVAL71
AVAL75
ATYR88

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 600
ChainResidue
AASN68
AALA72
AILE100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU11

site_idSWS_FT_FI2
Number of Residues1
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
AASP20

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU32
APHE104

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER117
AASN132

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU11proton shuttle (general acid/base)
AASP20covalent catalysis

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PDB entries from 2024-04-24

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