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6RXM

Crystal structure of CobB Ac2 (A76G, I131C, V162G) 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
C0036054molecular_functionprotein-malonyllysine demalonylase activity
C0036055molecular_functionprotein-succinyllysine desuccinylase activity
C0070403molecular_functionNAD+ binding
D0036054molecular_functionprotein-malonyllysine demalonylase activity
D0036055molecular_functionprotein-succinyllysine desuccinylase activity
D0070403molecular_functionNAD+ binding
E0036054molecular_functionprotein-malonyllysine demalonylase activity
E0036055molecular_functionprotein-succinyllysine desuccinylase activity
E0070403molecular_functionNAD+ binding
F0036054molecular_functionprotein-malonyllysine demalonylase activity
F0036055molecular_functionprotein-succinyllysine desuccinylase activity
F0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 300
ChainResidue
ACYS155
ASER158
ACYS174
ACYS176
ACYS177

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN B 301
ChainResidue
BCYS177
BCYS155
BGLN157
BCYS174
BCYS176

site_idAC3
Number of Residues5
Detailsbinding site for residue ZN C 300
ChainResidue
CCYS155
CSER158
CCYS174
CCYS176
CCYS177

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN D 301
ChainResidue
DCYS155
DCYS174
DCYS176
DCYS177

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN E 301
ChainResidue
ECYS155
ESER158
ECYS174
ECYS176
ECYS177

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN F 301
ChainResidue
FCYS155
FSER158
FCYS174
FCYS176
FCYS177

Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
GGLY14-HIS18

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsDNA_BIND:
ChainResidueDetails
GALY16-LYS20
HALY16-LYS20
IALY16-LYS20
JALY16-LYS20
KALY16-LYS20
LALY16-LYS20

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:22343720
ChainResidueDetails
GLYS12
BALA258
CGLY48
CGLN129
CGLY214
CASN240
CALA258
DGLY48
DGLN129
DGLY214
DASN240
HLYS12
DALA258
EGLY48
EGLN129
EGLY214
EASN240
EALA258
FGLY48
FGLN129
FGLY214
FASN240
ILYS12
FALA258
JLYS12
KLYS12
LLYS12
BGLN129
BGLY214
BASN240

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11080160, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592, ECO:0000269|PubMed:19113941
ChainResidueDetails
GALY16
EARG95
FTYR92
FARG95
HALY16
IALY16
JALY16
KALY16
LALY16
DTYR92
DARG95
ETYR92

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:15019790
ChainResidueDetails
ACYS155
ECYS174
FCYS155
FCYS174
ACYS174
BCYS155
BCYS174
CCYS155
CCYS174
DCYS155
DCYS174
ECYS155

223532

PDB entries from 2024-08-07

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