6RXR
Crystal structure of CobB Ac2 (A76G, I131C, V162G) in complex with H4K16Cr-2'OH-ADPr peptide intermediate after co-crystallisation
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 38 |
| Details | binding site for Di-peptide KMQ E 101 and LYS E 16 |
| Chain | Residue |
| A | GLY48 |
| A | HIS147 |
| A | VAL187 |
| A | VAL188 |
| A | TRP189 |
| A | PHE190 |
| A | GLY191 |
| A | GLU192 |
| A | GLY214 |
| A | THR215 |
| A | SER216 |
| A | ALA49 |
| A | VAL219 |
| A | TYR220 |
| A | ASN240 |
| A | LEU241 |
| A | GLU242 |
| A | PRO257 |
| A | ALA258 |
| A | HOH306 |
| A | HOH312 |
| A | HOH317 |
| A | GLY50 |
| A | HOH318 |
| E | ALA15 |
| E | ARG17 |
| E | HOH204 |
| E | HOH207 |
| E | HOH208 |
| E | HOH209 |
| E | HOH210 |
| E | HOH211 |
| A | ALA53 |
| A | GLU54 |
| A | PHE60 |
| A | TRP67 |
| A | GLN129 |
| A | CYS131 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | binding site for Di-peptide KMQ F 101 and LYS F 16 |
| Chain | Residue |
| B | GLY48 |
| B | ALA49 |
| B | GLY50 |
| B | ALA53 |
| B | GLU54 |
| B | PHE60 |
| B | TRP67 |
| B | GLN129 |
| B | CYS131 |
| B | HIS147 |
| B | VAL187 |
| B | VAL188 |
| B | PHE190 |
| B | GLY191 |
| B | GLU192 |
| B | GLY214 |
| B | THR215 |
| B | SER216 |
| B | VAL219 |
| B | TYR220 |
| B | ASN240 |
| B | LEU241 |
| B | GLU242 |
| B | ALA258 |
| B | HOH318 |
| B | HOH323 |
| B | HOH384 |
| F | ALA15 |
| F | ARG17 |
| F | HOH203 |
| F | HOH205 |
| F | HOH208 |
| F | HOH210 |
| F | HOH212 |
| F | HOH213 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | binding site for Di-peptide KMQ G 101 and LYS G 16 |
| Chain | Residue |
| C | HOH313 |
| C | HOH316 |
| C | HOH318 |
| G | ALA15 |
| G | ARG17 |
| G | HOH202 |
| G | HOH203 |
| G | HOH206 |
| G | HOH208 |
| G | HOH209 |
| C | GLY48 |
| C | ALA49 |
| C | GLY50 |
| C | ALA53 |
| C | GLU54 |
| C | PHE60 |
| C | TRP67 |
| C | GLN129 |
| C | CYS131 |
| C | HIS147 |
| C | VAL187 |
| C | VAL188 |
| C | TRP189 |
| C | PHE190 |
| C | GLY191 |
| C | GLU192 |
| C | GLY214 |
| C | THR215 |
| C | SER216 |
| C | VAL219 |
| C | TYR220 |
| C | ASN240 |
| C | LEU241 |
| C | GLU242 |
| C | PRO257 |
| C | ALA258 |
| site_id | AC4 |
| Number of Residues | 35 |
| Details | binding site for Di-peptide KMQ H 101 and LYS H 16 |
| Chain | Residue |
| D | GLY48 |
| D | ALA49 |
| D | GLY50 |
| D | ALA53 |
| D | GLU54 |
| D | PHE60 |
| D | TRP67 |
| D | GLN129 |
| D | CYS131 |
| D | HIS147 |
| D | VAL187 |
| D | VAL188 |
| D | TRP189 |
| D | PHE190 |
| D | GLY191 |
| D | GLU192 |
| D | GLY214 |
| D | THR215 |
| D | SER216 |
| D | VAL219 |
| D | TYR220 |
| D | ASN240 |
| D | LEU241 |
| D | GLU242 |
| D | ALA258 |
| D | HOH317 |
| D | HOH318 |
| D | HOH387 |
| H | ALA15 |
| H | ARG17 |
| H | HOH202 |
| H | HOH205 |
| H | HOH207 |
| H | HOH209 |
| H | HOH210 |
Functional Information from PROSITE/UniProt
| site_id | PS00047 |
| Number of Residues | 5 |
| Details | HISTONE_H4 Histone H4 signature. GAKRH |
| Chain | Residue | Details |
| E | GLY14-HIS18 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01121","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 108 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01121","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01121","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24176774","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01121","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15019790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | DNA binding: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"11080160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15150415","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17289592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19113941","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
