3K2G
Crystal structure of a Resiniferatoxin-binding protein from Rhodobacter sphaeroides
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008081 | molecular_function | phosphoric diester hydrolase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009056 | biological_process | catabolic process |
A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
A | 0046872 | molecular_function | metal ion binding |
B | 0008081 | molecular_function | phosphoric diester hydrolase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0009056 | biological_process | catabolic process |
B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
B | 0046872 | molecular_function | metal ion binding |
C | 0008081 | molecular_function | phosphoric diester hydrolase activity |
C | 0008270 | molecular_function | zinc ion binding |
C | 0009056 | biological_process | catabolic process |
C | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
C | 0046872 | molecular_function | metal ion binding |
D | 0008081 | molecular_function | phosphoric diester hydrolase activity |
D | 0008270 | molecular_function | zinc ion binding |
D | 0009056 | biological_process | catabolic process |
D | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 400 |
Chain | Residue |
A | HIS32 |
A | HIS34 |
A | GLU175 |
A | ASP302 |
A | ZN401 |
A | HOH872 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | HIS236 |
A | HOH372 |
A | ZN400 |
A | HOH872 |
A | TYR134 |
A | GLU175 |
A | HIS207 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 500 |
Chain | Residue |
A | HOH363 |
A | HOH366 |
A | HOH367 |
A | HOH369 |
A | HOH370 |
A | HOH371 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DTV A 402 |
Chain | Residue |
A | CYS39 |
A | TRP42 |
A | PHE72 |
A | TYR134 |
A | LEU135 |
A | PHE304 |
A | HOH610 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN B 400 |
Chain | Residue |
B | HIS32 |
B | HIS34 |
B | GLU175 |
B | ASP302 |
B | HOH363 |
B | ZN401 |
B | HOH870 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN B 401 |
Chain | Residue |
B | TYR134 |
B | GLU175 |
B | HIS207 |
B | HIS236 |
B | HOH363 |
B | ZN400 |
B | HOH772 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DTV B 402 |
Chain | Residue |
B | CYS39 |
B | PHE72 |
B | TYR134 |
B | PHE304 |
B | HOH870 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN C 400 |
Chain | Residue |
C | HIS32 |
C | HIS34 |
C | GLU175 |
C | ASP302 |
C | HOH364 |
C | ZN401 |
C | HOH869 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN C 401 |
Chain | Residue |
C | TYR134 |
C | GLU175 |
C | HIS207 |
C | HIS236 |
C | HOH363 |
C | HOH364 |
C | ZN400 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DTV C 402 |
Chain | Residue |
C | CYS39 |
C | TRP42 |
C | PHE72 |
C | TYR134 |
C | LEU135 |
C | HOH869 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN D 400 |
Chain | Residue |
D | HIS32 |
D | HIS34 |
D | GLU175 |
D | ASP302 |
D | HOH365 |
D | ZN401 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN D 401 |
Chain | Residue |
D | TYR134 |
D | GLU175 |
D | HIS207 |
D | HIS236 |
D | HOH364 |
D | HOH365 |
D | ZN400 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DTV D 402 |
Chain | Residue |
D | CYS39 |
D | TRP42 |
D | PHE72 |
D | TYR134 |
D | PHE304 |
D | HOH871 |
Functional Information from PROSITE/UniProt
site_id | PS01322 |
Number of Residues | 9 |
Details | PHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GhTLmHEHL |
Chain | Residue | Details |
A | GLY27-LEU35 |