6OFC
Crystal structure of M. tuberculosis glutamine-dependent NAD+ synthetase complexed with Sulfonamide derivative 1, pyrophosphate, and glutamine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008795 | molecular_function | NAD+ synthase activity |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0009435 | biological_process | NAD biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008795 | molecular_function | NAD+ synthase activity |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| B | 0009435 | biological_process | NAD biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| C | 0004359 | molecular_function | glutaminase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008795 | molecular_function | NAD+ synthase activity |
| C | 0009274 | cellular_component | peptidoglycan-based cell wall |
| C | 0009435 | biological_process | NAD biosynthetic process |
| C | 0016874 | molecular_function | ligase activity |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| D | 0004359 | molecular_function | glutaminase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008795 | molecular_function | NAD+ synthase activity |
| D | 0009274 | cellular_component | peptidoglycan-based cell wall |
| D | 0009435 | biological_process | NAD biosynthetic process |
| D | 0016874 | molecular_function | ligase activity |
| D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue SFH A 701 |
| Chain | Residue |
| A | GLY366 |
| A | TRP490 |
| A | SER491 |
| A | THR492 |
| A | ASP497 |
| A | HOH803 |
| A | VAL367 |
| A | SER368 |
| A | SER373 |
| A | PHE397 |
| A | ALA398 |
| A | LEU399 |
| A | ARG462 |
| A | THR480 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue SFH A 702 |
| Chain | Residue |
| A | ASN456 |
| A | THR492 |
| A | TYR493 |
| A | PHE634 |
| A | LYS635 |
| A | SER661 |
| D | ARG354 |
| D | LEU358 |
| D | ASN471 |
| D | GLY475 |
| D | HIS501 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue SFH A 703 |
| Chain | Residue |
| A | ARG354 |
| A | LEU358 |
| A | ASN471 |
| A | GLY475 |
| A | ILE476 |
| A | HIS501 |
| D | ASN456 |
| D | GLY489 |
| D | SER491 |
| D | THR492 |
| D | TYR493 |
| D | ARG627 |
| D | PHE631 |
| D | PHE634 |
| D | LYS635 |
| D | SER661 |
| D | SFH701 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 705 |
| Chain | Residue |
| A | MET663 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue SFH B 701 |
| Chain | Residue |
| B | GLY366 |
| B | VAL367 |
| B | SER368 |
| B | SER373 |
| B | PHE397 |
| B | ALA398 |
| B | LEU399 |
| B | ARG462 |
| B | THR480 |
| B | TRP490 |
| B | SER491 |
| B | THR492 |
| B | ASP497 |
| B | GLU552 |
| B | POP705 |
| B | HOH806 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue SFH B 702 |
| Chain | Residue |
| B | ASN456 |
| B | THR492 |
| B | TYR493 |
| B | PHE631 |
| B | PHE634 |
| B | LYS635 |
| B | SER661 |
| B | HOH807 |
| C | ARG354 |
| C | LEU358 |
| C | ASN471 |
| C | GLY475 |
| C | HIS501 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue SFH B 703 |
| Chain | Residue |
| B | ARG354 |
| B | LEU358 |
| B | ASN471 |
| B | GLY475 |
| B | ILE476 |
| B | HIS501 |
| C | ASN456 |
| C | TYR493 |
| C | PHE634 |
| C | LYS635 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 704 |
| Chain | Residue |
| B | MET499 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue POP B 705 |
| Chain | Residue |
| B | SER368 |
| B | GLY370 |
| B | LEU371 |
| B | ASP372 |
| B | SER373 |
| B | GLU541 |
| B | GLU552 |
| B | GLU553 |
| B | LEU554 |
| B | SFH701 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue GLN B 706 |
| Chain | Residue |
| B | ARG218 |
| D | LEU215 |
| D | ARG218 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 707 |
| Chain | Residue |
| A | ASP656 |
| B | ASP62 |
| B | ARG134 |
| A | ARG128 |
| A | ARG285 |
| A | LEU575 |
| site_id | AD3 |
| Number of Residues | 13 |
| Details | binding site for residue SFH C 701 |
| Chain | Residue |
| C | GLY366 |
| C | VAL367 |
| C | SER368 |
| C | SER373 |
| C | PHE397 |
| C | ALA398 |
| C | LEU399 |
| C | ARG462 |
| C | THR480 |
| C | TRP490 |
| C | SER491 |
| C | THR492 |
| C | ASP497 |
| site_id | AD4 |
| Number of Residues | 12 |
| Details | binding site for residue GLN C 702 |
| Chain | Residue |
| C | GLU52 |
| C | TYR58 |
| C | LYS121 |
| C | PRO125 |
| C | TYR127 |
| C | PHE130 |
| C | ALA176 |
| C | GLU177 |
| C | PHE180 |
| C | SER203 |
| C | ARG209 |
| C | HOH801 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue SFH D 701 |
| Chain | Residue |
| A | SFH703 |
| D | GLY366 |
| D | VAL367 |
| D | SER368 |
| D | PHE397 |
| D | LEU399 |
| D | ARG462 |
| D | THR480 |
| D | TRP490 |
| D | THR492 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 702 |
| Chain | Residue |
| D | THR463 |
| D | ASP497 |
| D | MET499 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue GLN D 703 |
| Chain | Residue |
| D | TYR127 |
| D | GLU177 |
| D | PHE180 |
| D | SER203 |
| D | ARG209 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 704 |
| Chain | Residue |
| A | LEU65 |
| A | ARG134 |
| B | ARG128 |
| D | ARG285 |
| D | LEU575 |
| D | ASP656 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor; for glutaminase activity => ECO:0000255|HAMAP-Rule:MF_02090, ECO:0000305|PubMed:15748981, ECO:0000305|PubMed:19270703 |
| Chain | Residue | Details |
| A | GLU52 | |
| B | GLU52 | |
| C | GLU52 | |
| D | GLU52 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: For glutaminase activity => ECO:0000255|HAMAP-Rule:MF_02090, ECO:0000305|PubMed:15748981, ECO:0000305|PubMed:19270703 |
| Chain | Residue | Details |
| A | LYS121 | |
| B | LYS121 | |
| C | LYS121 | |
| D | LYS121 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile; for glutaminase activity => ECO:0000255|HAMAP-Rule:MF_02090, ECO:0000305|PubMed:15748981, ECO:0000305|PubMed:19270703 |
| Chain | Residue | Details |
| A | ALA176 | |
| B | ALA176 | |
| C | ALA176 | |
| D | ALA176 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02090, ECO:0007744|PDB:3SYT |
| Chain | Residue | Details |
| A | TYR127 | |
| D | TYR127 | |
| D | SER203 | |
| D | ARG209 | |
| A | SER203 | |
| A | ARG209 | |
| B | TYR127 | |
| B | SER203 | |
| B | ARG209 | |
| C | TYR127 | |
| C | SER203 | |
| C | ARG209 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02090, ECO:0007744|PDB:3SEQ, ECO:0007744|PDB:3SEZ, ECO:0007744|PDB:3SYT, ECO:0007744|PDB:3SZG |
| Chain | Residue | Details |
| A | GLY366 | |
| B | GLY366 | |
| C | GLY366 | |
| D | GLY366 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_02090, ECO:0007744|PDB:3DLA, ECO:0007744|PDB:3SEQ, ECO:0007744|PDB:3SEZ, ECO:0007744|PDB:3SZG |
| Chain | Residue | Details |
| A | ASN456 | |
| B | ASN456 | |
| C | ASN456 | |
| D | ASN456 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02090, ECO:0007744|PDB:3SEQ, ECO:0007744|PDB:3SYT, ECO:0007744|PDB:3SZG |
| Chain | Residue | Details |
| A | THR480 | |
| B | THR480 | |
| C | THR480 | |
| D | THR480 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_02090, ECO:0007744|PDB:3SEQ, ECO:0007744|PDB:3SEZ, ECO:0007744|PDB:3SYT |
| Chain | Residue | Details |
| A | GLU485 | |
| B | GLU485 | |
| C | GLU485 | |
| D | GLU485 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_02090, ECO:0007744|PDB:3DLA, ECO:0007744|PDB:3SEQ, ECO:0007744|PDB:3SEZ, ECO:0007744|PDB:3SYT, ECO:0007744|PDB:3SZG |
| Chain | Residue | Details |
| A | TRP490 | |
| A | LYS635 | |
| B | TRP490 | |
| B | LYS635 | |
| C | TRP490 | |
| C | LYS635 | |
| D | TRP490 | |
| D | LYS635 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0007744|PDB:3DLA, ECO:0007744|PDB:3SEQ, ECO:0007744|PDB:3SEZ, ECO:0007744|PDB:3SYT, ECO:0007744|PDB:3SZG |
| Chain | Residue | Details |
| A | ARG354 | |
| C | ASN471 | |
| C | GLY475 | |
| C | HIS501 | |
| D | ARG354 | |
| D | ASN471 | |
| D | GLY475 | |
| D | HIS501 | |
| A | ASN471 | |
| A | GLY475 | |
| A | HIS501 | |
| B | ARG354 | |
| B | ASN471 | |
| B | GLY475 | |
| B | HIS501 | |
| C | ARG354 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0007744|PDB:3DLA, ECO:0007744|PDB:3SZG |
| Chain | Residue | Details |
| A | SER661 | |
| B | SER661 | |
| C | SER661 | |
| D | SER661 |
