2B4Y
Crystal Structure of Human Sirtuin homolog 5
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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | CYS166 |
| A | CYS169 |
| A | CYS207 |
| A | CYS212 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 2001 |
| Chain | Residue |
| B | CYS166 |
| B | CYS169 |
| B | CYS207 |
| B | CYS212 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 3001 |
| Chain | Residue |
| C | CYS169 |
| C | CYS207 |
| C | CYS212 |
| C | CYS166 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 4001 |
| Chain | Residue |
| D | CYS166 |
| D | CYS169 |
| D | CYS207 |
| D | CYS212 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE APR A 1002 |
| Chain | Residue |
| A | GLY58 |
| A | ALA59 |
| A | GLY60 |
| A | ALA63 |
| A | GLU64 |
| A | GLN140 |
| A | HIS158 |
| A | GLY249 |
| A | THR250 |
| A | SER251 |
| A | ASN275 |
| A | THR276 |
| A | GLU277 |
| A | PRO292 |
| A | CYS293 |
| A | EPE1003 |
| A | HOH1033 |
| A | HOH1070 |
| A | HOH1160 |
| A | HOH1176 |
| A | HOH1190 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE APR B 2002 |
| Chain | Residue |
| B | GLY58 |
| B | ALA59 |
| B | GLY60 |
| B | GLU64 |
| B | THR69 |
| B | GLN140 |
| B | HIS158 |
| B | GLY249 |
| B | THR250 |
| B | SER251 |
| B | ASN275 |
| B | THR276 |
| B | GLU277 |
| B | CYS293 |
| B | EPE2003 |
| B | HOH2028 |
| B | HOH2031 |
| B | HOH2160 |
| B | HOH2171 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE APR C 3002 |
| Chain | Residue |
| B | HOH2043 |
| C | GLY58 |
| C | ALA59 |
| C | GLY60 |
| C | ALA63 |
| C | GLU64 |
| C | THR69 |
| C | PHE70 |
| C | ARG71 |
| C | GLN140 |
| C | HIS158 |
| C | GLY249 |
| C | THR250 |
| C | SER251 |
| C | VAL254 |
| C | ASN275 |
| C | THR276 |
| C | GLU277 |
| C | PRO292 |
| C | CYS293 |
| C | EPE3003 |
| C | HOH3005 |
| C | HOH3067 |
| C | HOH3082 |
| C | HOH3145 |
| site_id | AC8 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE APR D 4002 |
| Chain | Residue |
| D | HOH4007 |
| D | HOH4039 |
| D | HOH4072 |
| D | HOH4128 |
| D | HOH4135 |
| D | GLY58 |
| D | ALA59 |
| D | GLY60 |
| D | GLU64 |
| D | THR69 |
| D | PHE70 |
| D | GLN140 |
| D | HIS158 |
| D | GLY249 |
| D | THR250 |
| D | SER251 |
| D | VAL254 |
| D | ASN275 |
| D | THR276 |
| D | GLU277 |
| D | PRO292 |
| D | CYS293 |
| D | EPE4003 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE EPE A 1003 |
| Chain | Residue |
| A | ALA82 |
| A | ALA86 |
| A | TYR102 |
| A | ARG105 |
| A | HIS158 |
| A | VAL221 |
| A | TRP222 |
| A | PHE223 |
| A | GLY224 |
| A | GLU225 |
| A | APR1002 |
| A | HOH1186 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EPE B 2003 |
| Chain | Residue |
| B | ALA82 |
| B | ALA86 |
| B | TYR102 |
| B | ARG105 |
| B | VAL221 |
| B | TRP222 |
| B | PHE223 |
| B | APR2002 |
| site_id | BC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE EPE C 3003 |
| Chain | Residue |
| C | PHE70 |
| C | ALA82 |
| C | ALA86 |
| C | ARG105 |
| C | HIS158 |
| C | VAL221 |
| C | PHE223 |
| C | GLU225 |
| C | LEU227 |
| C | APR3002 |
| C | HOH3144 |
| C | HOH3147 |
| D | SER168 |
| D | CYS169 |
| site_id | BC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE EPE D 4003 |
| Chain | Residue |
| C | SER168 |
| C | CYS169 |
| D | PHE70 |
| D | ALA82 |
| D | ALA86 |
| D | ARG105 |
| D | HIS158 |
| D | VAL221 |
| D | PHE223 |
| D | GLU225 |
| D | LEU227 |
| D | TYR255 |
| D | APR4002 |
| D | HOH4125 |
| D | HOH4149 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29180469","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03160","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03160","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22767592","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of human sirtuin homolog 5 in complex with NAD.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
