1L7D
Crystal Structure of R. rubrum Transhydrogenase Domain I without Bound NAD(H)
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 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 | GLN1332 | |
D | ASP1402 | |
D | GLY1434 | |
A | ARG127 | |
A | VAL180 | |
A | GLN247 | |
A | LEU266 | |
B | ARG527 | |
B | VAL580 | |
B | GLN647 | |
A | ASP202 | |
B | LEU666 | |
C | ARG927 | |
C | VAL980 | |
C | GLN1047 | |
C | LEU1066 | |
D | ARG1327 | |
D | VAL1380 | |
D | GLN1447 | |
D | LEU1466 | |
A | GLY234 | |
B | GLN532 | |
B | ASP602 | |
B | GLY634 | |
C | GLN932 | |
C | ASP1002 | |
C | GLY1034 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | VAL182 | |
B | VAL582 | |
C | VAL982 | |
D | VAL1382 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details |
Chain | Residue | Details |
A | ASP135 | |
A | SER138 | |
A | ARG127 | |
A | GLN132 |
site_id | CSA2 |
Number of Residues | 4 |
Details |
Chain | Residue | Details |
B | ARG527 | |
B | GLN532 | |
B | SER538 | |
B | ASP535 |
site_id | CSA3 |
Number of Residues | 4 |
Details |
Chain | Residue | Details |
C | SER938 | |
C | GLN932 | |
C | ASP935 | |
C | ARG927 |
site_id | CSA4 |
Number of Residues | 4 |
Details |
Chain | Residue | Details |
D | ASP1335 | |
D | ARG1327 | |
D | GLN1332 | |
D | SER1338 |
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 | ARG527 | hydrogen bond donor, steric role |
B | GLN532 | steric locator |
B | ASP535 | hydrogen bond acceptor, steric role |
B | SER538 | electrostatic stabiliser |
B | TYR635 | polar/non-polar interaction, steric role |
site_id | MCSA3 |
Number of Residues | 5 |
Details | M-CSA 116 |
Chain | Residue | Details |
C | ARG927 | hydrogen bond donor, steric role |
C | GLN932 | steric locator |
C | ASP935 | hydrogen bond acceptor, steric role |
C | SER938 | electrostatic stabiliser |
C | TYR1035 | polar/non-polar interaction, steric role |
site_id | MCSA4 |
Number of Residues | 5 |
Details | M-CSA 116 |
Chain | Residue | Details |
D | ARG1327 | hydrogen bond donor, steric role |
D | GLN1332 | steric locator |
D | ASP1335 | hydrogen bond acceptor, steric role |
D | SER1338 | electrostatic stabiliser |
D | TYR1435 | polar/non-polar interaction, steric role |