6RXM
Crystal structure of CobB Ac2 (A76G, I131C, V162G) in complex with H4K16-Acetyl peptide
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0036054 | molecular_function | protein-malonyllysine demalonylase activity |
A | 0036055 | molecular_function | protein-succinyllysine desuccinylase activity |
A | 0070403 | molecular_function | NAD+ binding |
B | 0036054 | molecular_function | protein-malonyllysine demalonylase activity |
B | 0036055 | molecular_function | protein-succinyllysine desuccinylase activity |
B | 0070403 | molecular_function | NAD+ binding |
C | 0036054 | molecular_function | protein-malonyllysine demalonylase activity |
C | 0036055 | molecular_function | protein-succinyllysine desuccinylase activity |
C | 0070403 | molecular_function | NAD+ binding |
D | 0036054 | molecular_function | protein-malonyllysine demalonylase activity |
D | 0036055 | molecular_function | protein-succinyllysine desuccinylase activity |
D | 0070403 | molecular_function | NAD+ binding |
E | 0036054 | molecular_function | protein-malonyllysine demalonylase activity |
E | 0036055 | molecular_function | protein-succinyllysine desuccinylase activity |
E | 0070403 | molecular_function | NAD+ binding |
F | 0036054 | molecular_function | protein-malonyllysine demalonylase activity |
F | 0036055 | molecular_function | protein-succinyllysine desuccinylase activity |
F | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue ZN A 300 |
Chain | Residue |
A | CYS155 |
A | SER158 |
A | CYS174 |
A | CYS176 |
A | CYS177 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue ZN B 301 |
Chain | Residue |
B | CYS177 |
B | CYS155 |
B | GLN157 |
B | CYS174 |
B | CYS176 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue ZN C 300 |
Chain | Residue |
C | CYS155 |
C | SER158 |
C | CYS174 |
C | CYS176 |
C | CYS177 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN D 301 |
Chain | Residue |
D | CYS155 |
D | CYS174 |
D | CYS176 |
D | CYS177 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue ZN E 301 |
Chain | Residue |
E | CYS155 |
E | SER158 |
E | CYS174 |
E | CYS176 |
E | CYS177 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue ZN F 301 |
Chain | Residue |
F | CYS155 |
F | SER158 |
F | CYS174 |
F | CYS176 |
F | CYS177 |
Functional Information from PROSITE/UniProt
site_id | PS00047 |
Number of Residues | 5 |
Details | HISTONE_H4 Histone H4 signature. GAKRH |
Chain | Residue | Details |
G | GLY14-HIS18 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | DNA_BIND: |
Chain | Residue | Details |
G | ALY16-LYS20 | |
H | ALY16-LYS20 | |
I | ALY16-LYS20 | |
J | ALY16-LYS20 | |
K | ALY16-LYS20 | |
L | ALY16-LYS20 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:22343720 |
Chain | Residue | Details |
G | LYS12 | |
B | ALA258 | |
C | GLY48 | |
C | GLN129 | |
C | GLY214 | |
C | ASN240 | |
C | ALA258 | |
D | GLY48 | |
D | GLN129 | |
D | GLY214 | |
D | ASN240 | |
H | LYS12 | |
D | ALA258 | |
E | GLY48 | |
E | GLN129 | |
E | GLY214 | |
E | ASN240 | |
E | ALA258 | |
F | GLY48 | |
F | GLN129 | |
F | GLY214 | |
F | ASN240 | |
I | LYS12 | |
F | ALA258 | |
J | LYS12 | |
K | LYS12 | |
L | LYS12 | |
B | GLN129 | |
B | GLY214 | |
B | ASN240 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11080160, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592, ECO:0000269|PubMed:19113941 |
Chain | Residue | Details |
G | ALY16 | |
E | ARG95 | |
F | TYR92 | |
F | ARG95 | |
H | ALY16 | |
I | ALY16 | |
J | ALY16 | |
K | ALY16 | |
L | ALY16 | |
D | TYR92 | |
D | ARG95 | |
E | TYR92 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:15019790 |
Chain | Residue | Details |
A | CYS155 | |
E | CYS174 | |
F | CYS155 | |
F | CYS174 | |
A | CYS174 | |
B | CYS155 | |
B | CYS174 | |
C | CYS155 | |
C | CYS174 | |
D | CYS155 | |
D | CYS174 | |
E | CYS155 |