2G2P
Crystal Structure of E.coli transthyretin-related protein with bound Zn and Br
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 | BR1021 |
A | HOH1109 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 1002 |
Chain | Residue |
B | HIS9 |
B | HIS98 |
B | BR1022 |
B | HOH1115 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 1003 |
Chain | Residue |
C | HIS98 |
C | BR1023 |
C | HOH1109 |
C | HIS9 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 1004 |
Chain | Residue |
D | HIS9 |
D | HIS98 |
D | BR1024 |
D | HOH1110 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1005 |
Chain | Residue |
A | HIS96 |
A | HIS98 |
A | SER114 |
A | HOH1141 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 1006 |
Chain | Residue |
B | HIS96 |
B | HIS98 |
B | SER114 |
B | HOH1141 |
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 | 3 |
Details | BINDING SITE FOR RESIDUE ZN D 1008 |
Chain | Residue |
D | HIS96 |
D | HIS98 |
D | SER114 |
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 D 1012 |
Chain | Residue |
D | GLN3 |
D | HIS96 |
D | SER114 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 1013 |
Chain | Residue |
A | ASP61 |
A | HIS89 |
A | HOH1136 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 1014 |
Chain | Residue |
B | ASP61 |
B | HIS89 |
B | HOH1144 |
D | ASP31 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN C 1015 |
Chain | Residue |
C | ASP61 |
C | HIS89 |
C | HOH1131 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 1016 |
Chain | Residue |
B | ASP31 |
D | ASP61 |
D | HIS89 |
D | HOH1107 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BR A 1021 |
Chain | Residue |
A | VAL8 |
A | ARG47 |
A | HIS98 |
A | ZN1001 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BR B 1022 |
Chain | Residue |
B | VAL8 |
B | ARG47 |
B | HIS98 |
B | ZN1002 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BR C 1023 |
Chain | Residue |
C | VAL8 |
C | ARG47 |
C | HIS98 |
C | ZN1003 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BR D 1024 |
Chain | Residue |
D | VAL8 |
D | ARG47 |
D | HIS98 |
D | ZN1004 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1100 |
Chain | Residue |
A | TRP34 |
A | ARG63 |
A | HOH1126 |
B | TRP34 |
B | ARG63 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 1101 |
Chain | Residue |
C | TRP34 |
C | ARG63 |
C | HOH1135 |
C | HOH1136 |
D | TRP34 |
D | ARG63 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1102 |
Chain | Residue |
A | TYR111 |
A | GLY113 |
A | SER114 |
C | HIS9 |
site_id | CC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 1103 |
Chain | Residue |
B | HIS9 |
B | SO41104 |
D | TYR111 |
D | GLY113 |
D | SER114 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 1104 |
Chain | Residue |
B | HIS98 |
B | PRO100 |
B | TYR111 |
B | GLY113 |
B | SER114 |
D | SO41103 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS9 | |
D | HIS9 | |
D | ARG47 | |
D | TYR111 | |
A | ARG47 | |
A | TYR111 | |
B | HIS9 | |
B | ARG47 | |
B | TYR111 | |
C | HIS9 | |
C | ARG47 | |
C | TYR111 |