1F8G
THE X-RAY STRUCTURE OF NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE FROM RHODOSPIRILLUM RUBRUM COMPLEXED WITH NAD+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003957 | molecular_function | NAD(P)+ transhydrogenase (Si-specific) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006740 | biological_process | NADPH regeneration |
| A | 0008750 | molecular_function | proton-translocating NAD(P)+ transhydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046983 | molecular_function | protein dimerization activity |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070403 | molecular_function | NAD+ binding |
| A | 0070404 | molecular_function | NADH binding |
| A | 1902600 | biological_process | proton transmembrane transport |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003957 | molecular_function | NAD(P)+ transhydrogenase (Si-specific) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0006740 | biological_process | NADPH regeneration |
| B | 0008750 | molecular_function | proton-translocating NAD(P)+ transhydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046983 | molecular_function | protein dimerization activity |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070403 | molecular_function | NAD+ binding |
| B | 0070404 | molecular_function | NADH binding |
| B | 1902600 | biological_process | proton transmembrane transport |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003957 | molecular_function | NAD(P)+ transhydrogenase (Si-specific) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0006740 | biological_process | NADPH regeneration |
| C | 0008750 | molecular_function | proton-translocating NAD(P)+ transhydrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046983 | molecular_function | protein dimerization activity |
| C | 0051287 | molecular_function | NAD binding |
| C | 0070403 | molecular_function | NAD+ binding |
| C | 0070404 | molecular_function | NADH binding |
| C | 1902600 | biological_process | proton transmembrane transport |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003957 | molecular_function | NAD(P)+ transhydrogenase (Si-specific) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0006740 | biological_process | NADPH regeneration |
| D | 0008750 | molecular_function | proton-translocating NAD(P)+ transhydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046983 | molecular_function | protein dimerization activity |
| D | 0051287 | molecular_function | NAD binding |
| D | 0070403 | molecular_function | NAD+ binding |
| D | 0070404 | molecular_function | NADH binding |
| D | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD A 2500 |
| Chain | Residue |
| A | ARG127 |
| A | GLY234 |
| A | ALA236 |
| A | GLN247 |
| A | THR264 |
| A | ALA265 |
| A | LEU266 |
| A | LEU275 |
| A | HOH2506 |
| A | HOH2526 |
| A | HOH2551 |
| A | ASP135 |
| A | HOH2563 |
| A | HOH2589 |
| A | HOH2705 |
| A | GLY179 |
| A | VAL180 |
| A | GLY181 |
| A | VAL182 |
| A | ASP202 |
| A | VAL203 |
| A | ARG204 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD B 2501 |
| Chain | Residue |
| B | GLY179 |
| B | VAL180 |
| B | GLY181 |
| B | VAL182 |
| B | ASP202 |
| B | VAL203 |
| B | ARG204 |
| B | GLY234 |
| B | TYR235 |
| B | ALA236 |
| B | GLN247 |
| B | THR264 |
| B | ALA265 |
| B | LEU266 |
| B | PRO273 |
| B | LEU275 |
| B | HOH2533 |
| B | HOH2537 |
| B | HOH2569 |
| B | HOH2571 |
| B | HOH2592 |
| B | HOH2662 |
| B | HOH2700 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD C 2502 |
| Chain | Residue |
| C | VAL180 |
| C | GLY181 |
| C | VAL182 |
| C | ASP202 |
| C | VAL203 |
| C | ARG204 |
| C | GLY234 |
| C | TYR235 |
| C | ALA236 |
| C | GLN247 |
| C | THR264 |
| C | ALA265 |
| C | LEU266 |
| C | PRO273 |
| C | LEU275 |
| C | HOH2513 |
| C | HOH2553 |
| C | HOH2586 |
| C | HOH2598 |
| C | HOH2603 |
| C | HOH2640 |
| C | HOH2650 |
| C | HOH2701 |
| C | HOH2817 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD D 2503 |
| Chain | Residue |
| D | ARG127 |
| D | GLN132 |
| D | SER138 |
| D | GLY179 |
| D | GLY181 |
| D | VAL182 |
| D | ASP202 |
| D | VAL203 |
| D | ARG204 |
| D | GLU230 |
| D | GLY234 |
| D | TYR235 |
| D | ALA236 |
| D | GLN247 |
| D | THR264 |
| D | ALA265 |
| D | LEU266 |
| D | LEU275 |
| D | HOH2511 |
| D | HOH2537 |
| D | HOH2559 |
| D | HOH2573 |
| D | HOH2584 |
| D | HOH2744 |
Functional Information from PROSITE/UniProt
| site_id | PS00836 |
| Number of Residues | 27 |
| Details | ALADH_PNT_1 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 1. AIPkErrpGEd..RVAiSPeVVkkLvGlG |
| Chain | Residue | Details |
| A | ALA4-GLY30 |
| site_id | PS00837 |
| Number of Residues | 26 |
| Details | ALADH_PNT_2 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 2. VFGVGvAGlqAiatAkRLGAvVmatD |
| Chain | Residue | Details |
| A | VAL177-ASP202 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609 |
| Chain | Residue | Details |
| A | GLN132 | |
| D | GLN132 | |
| D | ASP202 | |
| D | GLY234 | |
| A | ARG127 | |
| A | VAL180 | |
| A | GLN247 | |
| A | LEU266 | |
| B | ARG127 | |
| B | VAL180 | |
| B | GLN247 | |
| A | ASP202 | |
| B | LEU266 | |
| C | ARG127 | |
| C | VAL180 | |
| C | GLN247 | |
| C | LEU266 | |
| D | ARG127 | |
| D | VAL180 | |
| D | GLN247 | |
| D | LEU266 | |
| A | GLY234 | |
| B | GLN132 | |
| B | ASP202 | |
| B | GLY234 | |
| C | GLN132 | |
| C | ASP202 | |
| C | GLY234 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | VAL182 | |
| B | VAL182 | |
| C | VAL182 | |
| D | VAL182 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 116 |
| Chain | Residue | Details |
| A | ARG127 | hydrogen bond donor, steric role |
| A | GLN132 | steric locator |
| A | ASP135 | hydrogen bond acceptor, steric role |
| A | SER138 | electrostatic stabiliser |
| A | TYR235 | polar/non-polar interaction, steric role |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 116 |
| Chain | Residue | Details |
| B | ARG127 | hydrogen bond donor, steric role |
| B | GLN132 | steric locator |
| B | ASP135 | hydrogen bond acceptor, steric role |
| B | SER138 | electrostatic stabiliser |
| B | TYR235 | polar/non-polar interaction, steric role |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 116 |
| Chain | Residue | Details |
| C | ARG127 | hydrogen bond donor, steric role |
| C | GLN132 | steric locator |
| C | ASP135 | hydrogen bond acceptor, steric role |
| C | SER138 | electrostatic stabiliser |
| C | TYR235 | polar/non-polar interaction, steric role |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 116 |
| Chain | Residue | Details |
| D | ARG127 | hydrogen bond donor, steric role |
| D | GLN132 | steric locator |
| D | ASP135 | hydrogen bond acceptor, steric role |
| D | SER138 | electrostatic stabiliser |
| D | TYR235 | polar/non-polar interaction, steric role |
