Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8Q1X

Structural analysis of PLD3 reveals insights into the mechanism of lysosomal 5' exonuclease-mediated nucleic acid degradation

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
B0003824molecular_functioncatalytic activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU00153
ChainResidueDetails
AHIS201
BHIS201

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00153
ChainResidueDetails
ALYS203
AASP208
BLYS203
BASP208

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:O35405
ChainResidueDetails
AHIS416
BHIS416

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O35405
ChainResidueDetails
AHIS201
ALYS203
AASN218
AHIS416
BHIS201
BLYS203
BASN218
BHIS416

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:37994783, ECO:0007744|PDB:8Q1X
ChainResidueDetails
APHE438
BPHE438

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Cleavage; by lysosomal cysteine proteases => ECO:0000305|PubMed:29386126, ECO:0000305|PubMed:37994783
ChainResidueDetails
AASN71
BASN71

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:37994783
ChainResidueDetails
AASN97
AASN132
BASN97
BASN132

site_idSWS_FT_FI8
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:37994783
ChainResidueDetails
AASN236
AASN284
AASN387
BASN236
BASN284
BASN387

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon