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4PJ2

Crystal structure of Aeromonas hydrophila PliI in complex with Meretrix lusoria lysozyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0046872molecular_functionmetal ion binding
B0046872molecular_functionmetal ion binding
C0003796molecular_functionlysozyme activity
C0003824molecular_functioncatalytic activity
C0004568molecular_functionchitinase activity
C0005576cellular_componentextracellular region
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0031640biological_processkilling of cells of another organism
C0042742biological_processdefense response to bacterium
D0003796molecular_functionlysozyme activity
D0003824molecular_functioncatalytic activity
D0004568molecular_functionchitinase activity
D0005576cellular_componentextracellular region
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0031640biological_processkilling of cells of another organism
D0042742biological_processdefense response to bacterium
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue GOL A 201
ChainResidue
ASER38
BASP51
BARG53
AARG41
AASP51
AARG53
AHOH348
AHOH355
AHOH415
BSER38
BARG41

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 202
ChainResidue
AASP65
AGLN66
AHOH352
AHOH434
BTHR47
CTYR76
CTRP79
CALA80

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 203
ChainResidue
AASP86
AASN88
AASP90
AGLN92
AGLU94

site_idAC4
Number of Residues7
Detailsbinding site for residue MG B 201
ChainResidue
BLEU29
BPRO30
BSER31
BLYS91
BGLN92
BPRO93
BHOH301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01257
ChainResidueDetails
CGLU18
DGLU18

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01257
ChainResidueDetails
CASP29
DASP29

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:24192349, ECO:0000305|Ref.2, ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ
ChainResidueDetails
CLYS41
CTYR72
CHIS93
CLYS102
DLYS41
DTYR72
DHIS93
DLYS102

237992

PDB entries from 2025-06-25

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