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

2H2F

The Structural basis for Sirtuin Substrate affinity

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006338biological_processchromatin remodeling
A0008270molecular_functionzinc ion binding
A0016740molecular_functiontransferase activity
A0017136molecular_functionNAD-dependent histone deacetylase activity
A0034979molecular_functionNAD-dependent protein lysine deacetylase activity
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
A0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
ACYS124
ACYS127
ACYS148
ACYS151

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-methyllysine; by SETD7 => ECO:0000269|PubMed:15525938, ECO:0000269|PubMed:16415881
ChainResidueDetails
BLYS1

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:10656795
ChainResidueDetails
BLYS2
AGLY216
AASP231
AVAL232
ATHR26
AARG34
AGLN98
AHIS116
ASER189
ASER190
AASN214
ALEU215

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:29474172, ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS10
AILE100
AASP101

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-methyllysine; by KMT5A; alternate => ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287
ChainResidueDetails
BLYS11
ACYS127
ACYS148
ACYS151

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:11124955, ECO:0000269|PubMed:22214662, ECO:0000269|Ref.37
ChainResidueDetails
BLYS15

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon