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

6HMN

POLYADPRIBOSYL GLYCOSIDASE IN COMPLEX WITH PDD00014909

Functional Information from GO Data
ChainGOidnamespacecontents
A0004649molecular_functionpoly(ADP-ribose) glycohydrolase activity
A0005975biological_processcarbohydrate metabolic process
A0006282biological_processregulation of DNA repair
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue DMS A 1001
ChainResidue
AILE484
AVAL486
AASP487
APHE498

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 1002
ChainResidue
AASP927
ALYS930
AGLU709
AARG710
ACYS711
AGLU712
ATHR924

site_idAC3
Number of Residues8
Detailsbinding site for residue 70J A 1003
ChainResidue
ATHR725
AILE726
AGLU727
AGLN754
AARG758
ATYR792
ATYR795
APHE902

site_idAC4
Number of Residues7
Detailsbinding site for residue SO4 A 1004
ChainResidue
ATYR521
AARG535
ALEU538
ALYS559
ATYR560
AASN561
AVAL562

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 A 1005
ChainResidue
AARG535
ATYR564
AARG644
AARG645
AASN646
AARG941

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:23251397
ChainResidueDetails
AASP737

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:23251397
ChainResidueDetails
AGLU755
AGLU756

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:23251397, ECO:0000269|PubMed:30472116
ChainResidueDetails
AILE726
AASN740
AGLN754
AASN869

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9QYM2
ChainResidueDetails
ATYR795

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER448

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon