3G1P
Crystals structure of PhnP from E.coli K-12
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019700 | biological_process | organic phosphonate catabolic process |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0103043 | molecular_function | 5-phospho-alpha-D-ribosyl 1,2-cyclic phosphate phosphodiesterase activity |
| B | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019700 | biological_process | organic phosphonate catabolic process |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0103043 | molecular_function | 5-phospho-alpha-D-ribosyl 1,2-cyclic phosphate phosphodiesterase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 300 |
| Chain | Residue |
| A | CYS21 |
| A | CYS23 |
| A | CYS26 |
| A | HIS225 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 400 |
| Chain | Residue |
| A | MLT500 |
| A | HIS76 |
| A | HIS78 |
| A | HIS143 |
| A | ASP164 |
| A | MN401 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MN A 401 |
| Chain | Residue |
| A | ASP80 |
| A | HIS81 |
| A | ASP164 |
| A | HIS222 |
| A | HOH320 |
| A | MN400 |
| A | MLT500 |
| A | HOH573 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MLT A 500 |
| Chain | Residue |
| A | HIS76 |
| A | HIS78 |
| A | ASP80 |
| A | HIS143 |
| A | ASP164 |
| A | HIS200 |
| A | HOH324 |
| A | HOH391 |
| A | MN400 |
| A | MN401 |
| A | HOH486 |
| A | HOH573 |
| B | HOH265 |
| B | HOH509 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | CYS21 |
| B | CYS23 |
| B | CYS26 |
| B | HIS225 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 402 |
| Chain | Residue |
| B | HIS76 |
| B | HIS78 |
| B | HIS143 |
| B | ASP164 |
| B | MN403 |
| B | MLT501 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN B 403 |
| Chain | Residue |
| B | ASP80 |
| B | HIS81 |
| B | ASP164 |
| B | HIS222 |
| B | MN402 |
| B | MLT501 |
| B | HOH623 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE MLT B 501 |
| Chain | Residue |
| A | HOH338 |
| A | HOH612 |
| B | HIS76 |
| B | HIS78 |
| B | ASP80 |
| B | HIS143 |
| B | ASP164 |
| B | HIS200 |
| B | HOH339 |
| B | HOH356 |
| B | MN402 |
| B | MN403 |
| B | HOH529 |
| B | HOH575 |
| B | HOH613 |
| B | HOH623 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19366688, ECO:0000269|PubMed:21830807 |
| Chain | Residue | Details |
| A | CYS21 | |
| A | HIS222 | |
| A | HIS225 | |
| B | CYS21 | |
| B | CYS23 | |
| B | CYS26 | |
| B | HIS76 | |
| B | HIS78 | |
| B | ASP80 | |
| B | HIS81 | |
| B | HIS143 | |
| A | CYS23 | |
| B | ASP164 | |
| B | HIS222 | |
| B | HIS225 | |
| A | CYS26 | |
| A | HIS76 | |
| A | HIS78 | |
| A | ASP80 | |
| A | HIS81 | |
| A | HIS143 | |
| A | ASP164 |
