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4TWI

The structure of Sir2Af1 bound to a succinylated histone peptide

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
A0036054molecular_functionprotein-malonyllysine demalonylase activity
A0036055molecular_functionprotein-succinyllysine desuccinylase activity
A0046872molecular_functionmetal ion binding
A0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
ACYS124
ACYS127
ACYS145
ACYS148

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL B 101
ChainResidue
BARG6
BHIS7
BARG8
BHOH205

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsDNA_BIND:
ChainResidueDetails
BSLL5-LYS9

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:22343720
ChainResidueDetails
BLYS-3
BLYS1
AGLY185
AASN211
AALA229

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11080160, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592, ECO:0000269|PubMed:19113941
ChainResidueDetails
BSLL5
AARG67

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395
ChainResidueDetails
ACYS124
ACYS127
ACYS145
ACYS148

222415

PDB entries from 2024-07-10

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