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 | 0005886 | cellular_component | plasma membrane |
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 | 0050661 | molecular_function | NADP binding |
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 | 0005886 | cellular_component | plasma membrane |
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 | 0050661 | molecular_function | NADP binding |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 385 |
Chain | Residue |
A | ARG147 |
A | ARG326 |
B | TYR154 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 386 |
Chain | Residue |
A | THR169 |
A | PRO171 |
A | SO4386 |
B | ASP330 |
B | PRO333 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 385 |
Chain | Residue |
A | LYS316 |
B | ARG147 |
B | ARG326 |
A | TYR154 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 386 |
Chain | Residue |
A | ARG158 |
A | HOH501 |
A | HOH510 |
B | PRO333 |
B | SO4386 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAP C 400 |
Chain | Residue |
B | SER129 |
B | TXD600 |
C | GLY54 |
C | TYR55 |
C | GLY56 |
C | ALA60 |
C | VAL87 |
C | GLY89 |
C | ARG90 |
C | MET91 |
C | PRO92 |
C | GLY129 |
C | ALA130 |
C | ASN131 |
C | ASP132 |
C | VAL133 |
C | LYS164 |
C | ARG165 |
C | SER166 |
C | GLY170 |
C | TYR171 |
C | GLY189 |
C | ASP190 |
C | ALA191 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE TXD A 500 |
Chain | Residue |
A | ARG127 |
A | ILE128 |
A | GLN132 |
A | ASP135 |
A | GLY179 |
A | GLY181 |
A | VAL182 |
A | ASP202 |
A | VAL203 |
A | ARG204 |
A | GLY234 |
A | ALA236 |
A | GLN247 |
A | THR264 |
A | ALA265 |
A | LEU266 |
A | PRO273 |
A | LEU275 |
site_id | AC7 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE TXD B 600 |
Chain | Residue |
B | ARG127 |
B | ILE128 |
B | SER129 |
B | GLN132 |
B | SER138 |
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 | HOH607 |
C | TYR171 |
C | NAP400 |
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
Chain | Residue | Details |
A | GLN132 | |
A | LEU266 | |
B | ARG127 | |
B | VAL180 | |
B | GLN247 | |
B | LEU266 | |
A | ASP202 | |
A | GLY234 | |
B | GLN132 | |
B | ASP202 | |
B | GLY234 | |
A | ARG127 | |
A | VAL180 | |
A | GLN247 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | VAL182 | |
B | VAL182 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1djl |
Chain | Residue | Details |
C | ARG90 | |
C | TYR171 | |
C | TYR55 | |
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 |