3MDW
The structure of N-formimino-L-Glutamate Iminohydrolase from Pseudomonas aeruginosa complexed with N-formimino-L-Aspartate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006547 | biological_process | histidine metabolic process |
| A | 0006548 | biological_process | histidine catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0019239 | molecular_function | deaminase activity |
| A | 0019556 | biological_process | histidine catabolic process to glutamate and formamide |
| A | 0019557 | biological_process | histidine catabolic process to glutamate and formate |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050416 | molecular_function | formimidoylglutamate deiminase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006547 | biological_process | histidine metabolic process |
| B | 0006548 | biological_process | histidine catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0019239 | molecular_function | deaminase activity |
| B | 0019556 | biological_process | histidine catabolic process to glutamate and formamide |
| B | 0019557 | biological_process | histidine catabolic process to glutamate and formate |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050416 | molecular_function | formimidoylglutamate deiminase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006547 | biological_process | histidine metabolic process |
| C | 0006548 | biological_process | histidine catabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| C | 0019239 | molecular_function | deaminase activity |
| C | 0019556 | biological_process | histidine catabolic process to glutamate and formamide |
| C | 0019557 | biological_process | histidine catabolic process to glutamate and formate |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050416 | molecular_function | formimidoylglutamate deiminase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006547 | biological_process | histidine metabolic process |
| D | 0006548 | biological_process | histidine catabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| D | 0019239 | molecular_function | deaminase activity |
| D | 0019556 | biological_process | histidine catabolic process to glutamate and formamide |
| D | 0019557 | biological_process | histidine catabolic process to glutamate and formate |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050416 | molecular_function | formimidoylglutamate deiminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NFQ A 454 |
| Chain | Residue |
| A | HIS58 |
| A | ASP320 |
| A | HOH505 |
| A | HOH508 |
| A | HOH539 |
| A | HOH568 |
| A | HOH1026 |
| A | GLN61 |
| A | PHE78 |
| A | ARG82 |
| A | TYR121 |
| A | HIS206 |
| A | ARG209 |
| A | GLU235 |
| A | LEU298 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NFQ B 454 |
| Chain | Residue |
| B | GLN61 |
| B | PHE78 |
| B | ARG82 |
| B | TYR121 |
| B | HIS206 |
| B | ARG209 |
| B | GLU235 |
| B | LEU298 |
| B | ASP320 |
| B | HOH495 |
| B | HOH554 |
| B | HOH564 |
| B | HOH599 |
| B | HOH1021 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NFQ C 454 |
| Chain | Residue |
| C | HIS58 |
| C | GLN61 |
| C | ARG82 |
| C | TYR121 |
| C | HIS206 |
| C | ARG209 |
| C | GLU235 |
| C | LEU298 |
| C | ASP320 |
| C | HOH489 |
| C | HOH524 |
| C | HOH539 |
| C | HOH540 |
| C | HOH1024 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NFQ D 454 |
| Chain | Residue |
| D | HIS58 |
| D | GLN61 |
| D | PHE78 |
| D | ARG82 |
| D | TYR121 |
| D | HIS206 |
| D | ARG209 |
| D | GLU235 |
| D | LEU298 |
| D | ASP320 |
| D | HOH511 |
| D | HOH517 |
| D | HOH526 |
| D | HOH577 |
| D | HOH1023 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 455 |
| Chain | Residue |
| A | HIS56 |
| A | HIS58 |
| A | HIS232 |
| A | ASP320 |
| A | HOH1026 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 455 |
| Chain | Residue |
| B | HIS56 |
| B | HIS58 |
| B | HIS232 |
| B | ASP320 |
| B | HOH1021 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 455 |
| Chain | Residue |
| C | HIS56 |
| C | HIS58 |
| C | HIS232 |
| C | ASP320 |
| C | HOH1024 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 455 |
| Chain | Residue |
| D | HIS56 |
| D | HIS58 |
| D | HIS232 |
| D | ASP320 |
| D | HOH1023 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL C 456 |
| Chain | Residue |
| A | GLY179 |
| A | GLU181 |
| A | ALA182 |
| A | HOH533 |
| A | HOH809 |
| C | HIS161 |
| C | THR212 |
| C | GLN214 |
| C | GLN215 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 456 |
| Chain | Residue |
| A | LEU11 |
| A | PRO12 |
| A | ARG358 |
| A | ASP362 |
| A | GLY377 |
| A | SER378 |
| A | HOH469 |
| A | HOH483 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 D 456 |
| Chain | Residue |
| D | HIS161 |
| D | THR212 |
| D | GLN214 |
| D | GLN215 |
| D | HOH798 |
| B | GLY179 |
| B | GLU181 |
| B | ALA182 |
| B | HOH812 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17128965, ECO:0000305|PubMed:25559274 |
| Chain | Residue | Details |
| A | HIS269 | |
| A | ASP320 | |
| B | HIS269 | |
| B | ASP320 | |
| C | HIS269 | |
| C | ASP320 | |
| D | HIS269 | |
| D | ASP320 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25559274, ECO:0007744|PDB:3MDU, ECO:0007744|PDB:3MDW, ECO:0007744|PDB:4RDV, ECO:0007744|PDB:4RDW, ECO:0007744|PDB:4RZB |
| Chain | Residue | Details |
| A | HIS56 | |
| A | HIS58 | |
| A | HIS232 | |
| A | ASP320 | |
| B | HIS56 | |
| B | HIS58 | |
| B | HIS232 | |
| B | ASP320 | |
| C | HIS56 | |
| C | HIS58 | |
| C | HIS232 | |
| C | ASP320 | |
| D | HIS56 | |
| D | HIS58 | |
| D | HIS232 | |
| D | ASP320 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:25559274, ECO:0007744|PDB:3MDU, ECO:0007744|PDB:3MDW, ECO:0007744|PDB:4RDV, ECO:0007744|PDB:4RDW, ECO:0007744|PDB:4RZB |
| Chain | Residue | Details |
| A | GLN61 | |
| A | ARG82 | |
| A | TYR121 | |
| A | HIS206 | |
| A | ARG209 | |
| A | GLU235 | |
| B | GLN61 | |
| B | ARG82 | |
| B | TYR121 | |
| B | HIS206 | |
| B | ARG209 | |
| B | GLU235 | |
| C | GLN61 | |
| C | ARG82 | |
| C | TYR121 | |
| C | HIS206 | |
| C | ARG209 | |
| C | GLU235 | |
| D | GLN61 | |
| D | ARG82 | |
| D | TYR121 | |
| D | HIS206 | |
| D | ARG209 | |
| D | GLU235 |
