3ITG
Structure the proline utilization A proline dehydrogenase domain (PutA86-630) inactivated with N-propargylglycine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase (NAD+) activity |
| A | 0004657 | molecular_function | proline dehydrogenase activity |
| A | 0006562 | biological_process | L-proline catabolic process |
| B | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase (NAD+) activity |
| B | 0004657 | molecular_function | proline dehydrogenase activity |
| B | 0006562 | biological_process | L-proline catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FDA A 2001 |
| Chain | Residue |
| A | HOH8 |
| A | GLY435 |
| A | ALA436 |
| A | TYR437 |
| A | TRP438 |
| A | TYR456 |
| A | THR457 |
| A | ARG458 |
| A | LYS459 |
| A | THR462 |
| A | ALA485 |
| A | LYX329 |
| A | THR486 |
| A | HIS487 |
| A | ASN488 |
| A | GLN511 |
| A | CYS512 |
| A | LEU513 |
| A | TYR540 |
| A | ALA562 |
| A | ASN563 |
| A | SER565 |
| A | ASP370 |
| A | PHE566 |
| A | HOH717 |
| A | ALA371 |
| A | GLN404 |
| A | TYR406 |
| A | ARG431 |
| A | VAL433 |
| A | LYS434 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FDA B 2002 |
| Chain | Residue |
| B | HOH6 |
| B | LYX329 |
| B | ASP370 |
| B | ALA371 |
| B | GLN404 |
| B | TYR406 |
| B | ARG431 |
| B | VAL433 |
| B | LYS434 |
| B | GLY435 |
| B | ALA436 |
| B | TYR437 |
| B | TRP438 |
| B | TYR456 |
| B | THR457 |
| B | ARG458 |
| B | LYS459 |
| B | THR462 |
| B | ALA485 |
| B | THR486 |
| B | HIS487 |
| B | ASN488 |
| B | GLN511 |
| B | CYS512 |
| B | LEU513 |
| B | TYR540 |
| B | ALA562 |
| B | ASN563 |
| B | SER565 |
| B | PHE566 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q72IB8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2006","submissionDatabase":"PDB data bank","title":"Hydrogen Bonding Interactions of the 2-OH Ribityl Group and the N(5) Position of the FAD Cofactor Regulate PutA-membrane Associations in Escherichia coli.","authors":["Zhang W.","Zhang M.","Zhu W.","Wanduragula S.","Rewinkel D.","Tanner J.J.","Becker D.F."]}},{"source":"PubMed","id":"12514740","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15449943","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1TJ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TJ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FZN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4O8A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 34 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12514740","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15449943","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2006","submissionDatabase":"PDB data bank","title":"Hydrogen Bonding Interactions of the 2-OH Ribityl Group and the N(5) Position of the FAD Cofactor Regulate PutA-membrane Associations in Escherichia coli.","authors":["Zhang W.","Zhang M.","Zhu W.","Wanduragula S.","Rewinkel D.","Tanner J.J.","Becker D.F."]}},{"source":"PDB","id":"1TIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TJ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TJ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TJ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FZN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4O8A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2006","submissionDatabase":"PDB data bank","title":"Hydrogen Bonding Interactions of the 2-OH Ribityl Group and the N(5) Position of the FAD Cofactor Regulate PutA-membrane Associations in Escherichia coli.","authors":["Zhang W.","Zhang M.","Zhu W.","Wanduragula S.","Rewinkel D.","Tanner J.J.","Becker D.F."]}},{"source":"PDB","id":"2FZN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
