Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2DQA

Crystal Structure of Tapes japonica Lysozyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004568molecular_functionchitinase activity
A0005576cellular_componentextracellular region
A0008233molecular_functionpeptidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0042803molecular_functionprotein homodimerization activity
A0061929molecular_functiongamma-glutamylaminecyclotransferase activity
B0003796molecular_functionlysozyme activity
B0004568molecular_functionchitinase activity
B0005576cellular_componentextracellular region
B0008233molecular_functionpeptidase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0042803molecular_functionprotein homodimerization activity
B0061929molecular_functiongamma-glutamylaminecyclotransferase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01257, ECO:0000269|PubMed:17631496
ChainResidueDetails
AGLU18
BGLU18

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01257, ECO:0000269|PubMed:17631496
ChainResidueDetails
AASP30
BASP30

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:17631496, ECO:0007744|PDB:2DQA
ChainResidueDetails
ALYS42
BLYS108
ATYR73
ATYR81
AHIS94
ALYS108
BLYS42
BTYR73
BTYR81
BHIS94

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Cleavage => ECO:0000305|PubMed:14523554, ECO:0000305|PubMed:15249048, ECO:0000305|PubMed:9914527
ChainResidueDetails
ALYS123
BLYS123

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN64
BASN64

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon