2G2N
Crystal Structure of E.coli transthyretin-related protein with bound Zn
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006144 | biological_process | purine nucleobase metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0033971 | molecular_function | hydroxyisourate hydrolase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0006144 | biological_process | purine nucleobase metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0033971 | molecular_function | hydroxyisourate hydrolase activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0006144 | biological_process | purine nucleobase metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0033971 | molecular_function | hydroxyisourate hydrolase activity |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0006144 | biological_process | purine nucleobase metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0032991 | cellular_component | protein-containing complex |
| D | 0033971 | molecular_function | hydroxyisourate hydrolase activity |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | HIS9 |
| A | HIS98 |
| A | HOH1026 |
| A | HOH1027 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1002 |
| Chain | Residue |
| B | HIS9 |
| B | HIS98 |
| B | HOH1112 |
| B | HOH1113 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 1003 |
| Chain | Residue |
| C | HIS98 |
| C | HOH1107 |
| C | HOH1108 |
| C | HIS9 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 1004 |
| Chain | Residue |
| D | HIS9 |
| D | HIS98 |
| D | HOH1027 |
| D | HOH1028 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 1005 |
| Chain | Residue |
| A | HIS96 |
| A | HIS98 |
| A | SER114 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 1006 |
| Chain | Residue |
| B | HIS96 |
| B | HIS98 |
| B | SER114 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN C 1007 |
| Chain | Residue |
| C | HIS96 |
| C | HIS98 |
| C | SER114 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 1008 |
| Chain | Residue |
| D | HIS96 |
| D | HIS98 |
| D | SER114 |
| D | HOH1034 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN A 1009 |
| Chain | Residue |
| A | HIS96 |
| A | SER114 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN B 1010 |
| Chain | Residue |
| B | HIS96 |
| B | SER114 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 1013 |
| Chain | Residue |
| A | ASP61 |
| A | HIS89 |
| A | HOH1028 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1014 |
| Chain | Residue |
| B | ASP61 |
| B | HIS89 |
| B | HOH1114 |
| D | ASP31 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN C 1015 |
| Chain | Residue |
| C | ASP61 |
| C | HIS89 |
| C | HOH1110 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 1016 |
| Chain | Residue |
| B | ASP31 |
| D | ASP61 |
| D | HIS89 |
| D | HOH1030 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1017 |
| Chain | Residue |
| A | GLU83 |
| A | HOH1030 |
| B | GLU87 |
| B | HOH1117 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 1018 |
| Chain | Residue |
| A | GLU87 |
| A | HOH1029 |
| B | GLU83 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN C 1019 |
| Chain | Residue |
| C | GLU83 |
| D | GLU87 |
| D | HOH1031 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 1020 |
| Chain | Residue |
| C | GLU87 |
| D | GLU83 |
| D | HOH1032 |
| D | HOH1033 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1100 |
| Chain | Residue |
| A | TRP34 |
| A | ARG63 |
| B | TRP34 |
| B | ARG63 |
| B | HOH1167 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1101 |
| Chain | Residue |
| C | TRP34 |
| C | ARG63 |
| C | HOH1122 |
| C | HOH1141 |
| C | HOH1151 |
| D | TRP34 |
| D | ARG63 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
