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6RXJ

Crystal structure of CobB wt in complex with H4K16-Acetyl peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0036054molecular_functionprotein-malonyllysine demalonylase activity
A0036055molecular_functionprotein-succinyllysine desuccinylase activity
A0070403molecular_functionNAD+ binding
B0036054molecular_functionprotein-malonyllysine demalonylase activity
B0036055molecular_functionprotein-succinyllysine desuccinylase activity
B0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
ACYS155
ACYS174
ACYS176
ACYS177

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN B 301
ChainResidue
BCYS155
BCYS174
BCYS176
BCYS177
BHOH520

Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
CGLY14-HIS18

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsDNA_BIND:
ChainResidueDetails
CALY16-LYS20
DALY16-LYS20

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:22343720
ChainResidueDetails
AGLY214
AASN240
BGLY48
BGLN129
BGLY214
BASN240
CLYS12
DLYS12

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11080160, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592, ECO:0000269|PubMed:19113941
ChainResidueDetails
CALY16
DALY16
BTYR92
BARG95

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:15019790
ChainResidueDetails
ACYS155
ACYS174
BCYS155
BCYS174

221051

PDB entries from 2024-06-12

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