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1XJU

Crystal structure of secreted inactive form of P1 phage endolysin Lyz

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0009253biological_processpeptidoglycan catabolic process
A0016998biological_processcell wall macromolecule catabolic process
B0003796molecular_functionlysozyme activity
B0009253biological_processpeptidoglycan catabolic process
B0016998biological_processcell wall macromolecule catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 601
ChainResidue
BARG165
BLYS168
BHOH664
BHOH724
BHOH756
BHOH831
BHOH847

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
ALYS127
AALA128
AHOH677
AHOH824
AARG90
ASER126

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 603
ChainResidue
BSER136
BLYS139
BTRP140
BHIS152
BHOH912

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 604
ChainResidue
BHIS95
BARG122
BHIS138
BARG165
BHOH617
BHOH641
BHOH682
BHOH798

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 605
ChainResidue
BARG122
BHOH619
BHOH666
BHOH696
BHOH719
BHOH857
BHOH891

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 606
ChainResidue
AARG129
AGLU134
ALYS139
AHOH679
AHOH812

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 607
ChainResidue
BLYS99
BHOH826

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 608
ChainResidue
BARG29
BHOH692
BHOH829
BHOH870

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04136, ECO:0000305|PubMed:15637279
ChainResidueDetails
AGLU42
BGLU42

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04136, ECO:0000269|PubMed:15637279
ChainResidueDetails
ACYS51
BCYS51

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 206l
ChainResidueDetails
AGLU42
ACYS51

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 206l
ChainResidueDetails
BGLU42
BCYS51

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PDB entries from 2024-09-18

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