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1ZYT

Crystal structure of spin labeled T4 Lysozyme (A82R1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0009253biological_processpeptidoglycan catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
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 Residues2
DetailsBINDING SITE FOR RESIDUE MTN A 165
ChainResidue
AARG80
ACYS82

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE AZI A 200
ChainResidue
AHOH310
ALYS19
AARG125
ATRP126
AASP127
AGLU128
AHOH225
AHOH244

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 201
ChainResidue
ALYS124
ATHR142
AASN144
AARG145
AHOH274
AHOH285

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 202
ChainResidue
AASN132
ALYS135
AHOH228

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 203
ChainResidue
AHIS31
ALYS135
AHOH277

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HED A 180
ChainResidue
AILE3
APHE4
AASN68
AASP72
AVAL75
AVAL75
ATYR88
AALA93
AILE100
AHOH216

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_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 206l
ChainResidueDetails
AGLU11
AASP20

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

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PDB entries from 2024-11-06

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