2EQ9
Crystal structure of lipoamide dehydrogenase from thermus thermophilus HB8 with psbdb
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0016746 | molecular_function | acyltransferase activity |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
E | 0000166 | molecular_function | nucleotide binding |
E | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
F | 0016746 | molecular_function | acyltransferase activity |
G | 0000166 | molecular_function | nucleotide binding |
G | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
H | 0000166 | molecular_function | nucleotide binding |
H | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
I | 0016746 | molecular_function | acyltransferase activity |
J | 0000166 | molecular_function | nucleotide binding |
J | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
J | 0050660 | molecular_function | flavin adenine dinucleotide binding |
K | 0000166 | molecular_function | nucleotide binding |
K | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
K | 0016491 | molecular_function | oxidoreductase activity |
K | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
K | 0050660 | molecular_function | flavin adenine dinucleotide binding |
L | 0016746 | molecular_function | acyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 38 |
Details | BINDING SITE FOR RESIDUE FAD A 8482 |
Chain | Residue |
A | ILE15 |
A | CYS47 |
A | GLY51 |
A | CYS52 |
A | THR55 |
A | LYS56 |
A | GLY117 |
A | PHE118 |
A | ALA119 |
A | ALA146 |
A | THR147 |
A | GLY16 |
A | GLY148 |
A | SER166 |
A | ARG274 |
A | LEU281 |
A | GLY313 |
A | ASP314 |
A | LEU320 |
A | LEU321 |
A | ALA322 |
A | HIS323 |
A | GLY18 |
A | ALA325 |
A | TYR353 |
A | HOH8484 |
A | HOH8487 |
A | HOH8491 |
A | HOH8498 |
A | HOH8507 |
A | HOH8564 |
B | HIS446 |
A | PRO19 |
A | GLY20 |
A | GLU39 |
A | ALA40 |
A | GLU42 |
A | GLY45 |
site_id | AC2 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE FAD B 1482 |
Chain | Residue |
A | HIS446 |
B | ILE15 |
B | GLY16 |
B | GLY18 |
B | PRO19 |
B | GLY20 |
B | GLU39 |
B | ALA40 |
B | GLU42 |
B | GLY45 |
B | CYS47 |
B | GLY51 |
B | CYS52 |
B | THR55 |
B | LYS56 |
B | GLY117 |
B | PHE118 |
B | ALA119 |
B | ALA146 |
B | THR147 |
B | GLY148 |
B | SER166 |
B | ARG274 |
B | LEU281 |
B | GLY313 |
B | ASP314 |
B | LEU320 |
B | LEU321 |
B | ALA322 |
B | HIS323 |
B | TYR353 |
B | HOH1503 |
B | HOH1504 |
B | HOH1512 |
B | HOH1529 |
B | HOH1530 |
B | HOH1584 |
site_id | AC3 |
Number of Residues | 38 |
Details | BINDING SITE FOR RESIDUE FAD D 2482 |
Chain | Residue |
D | GLY313 |
D | ASP314 |
D | LEU320 |
D | LEU321 |
D | ALA322 |
D | HIS323 |
D | TYR353 |
D | HOH2491 |
D | HOH2493 |
D | HOH2496 |
D | HOH2503 |
D | HOH2504 |
D | HOH2575 |
E | HIS446 |
D | ILE15 |
D | GLY16 |
D | GLY18 |
D | PRO19 |
D | GLY20 |
D | GLU39 |
D | ALA40 |
D | GLU42 |
D | GLY45 |
D | CYS47 |
D | GLY51 |
D | CYS52 |
D | THR55 |
D | LYS56 |
D | GLY117 |
D | PHE118 |
D | ALA119 |
D | ALA146 |
D | THR147 |
D | GLY148 |
D | SER166 |
D | ARG274 |
D | ARG277 |
D | LEU281 |
site_id | AC4 |
Number of Residues | 38 |
Details | BINDING SITE FOR RESIDUE FAD E 3482 |
Chain | Residue |
D | HIS446 |
E | ILE15 |
E | GLY16 |
E | GLY18 |
E | PRO19 |
E | GLY20 |
E | GLU39 |
E | ALA40 |
E | GLU42 |
E | GLY45 |
E | CYS47 |
E | GLY51 |
E | CYS52 |
E | THR55 |
E | LYS56 |
E | GLY117 |
E | PHE118 |
E | ALA119 |
E | ALA146 |
E | THR147 |
E | GLY148 |
E | SER166 |
E | ARG274 |
E | ARG277 |
E | LEU281 |
E | GLY313 |
E | ASP314 |
E | LEU320 |
E | LEU321 |
E | ALA322 |
E | HIS323 |
E | TYR353 |
E | HOH3491 |
E | HOH3503 |
E | HOH3508 |
E | HOH3514 |
E | HOH3522 |
E | HOH3585 |
site_id | AC5 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE FAD G 4482 |
Chain | Residue |
G | ILE15 |
G | GLY16 |
G | GLY18 |
G | PRO19 |
G | GLY20 |
G | GLU39 |
G | ALA40 |
G | GLU42 |
G | GLY45 |
G | CYS47 |
G | GLY51 |
G | CYS52 |
G | LYS56 |
G | GLY117 |
G | PHE118 |
G | ALA119 |
G | ALA146 |
G | THR147 |
G | GLY148 |
G | SER166 |
G | ARG274 |
G | LEU281 |
G | GLY313 |
G | ASP314 |
G | LEU320 |
G | LEU321 |
G | ALA322 |
G | HIS323 |
G | TYR353 |
G | HOH4492 |
G | HOH4502 |
G | HOH4511 |
G | HOH4572 |
G | HOH4598 |
G | HOH4607 |
H | HIS446 |
site_id | AC6 |
Number of Residues | 39 |
Details | BINDING SITE FOR RESIDUE FAD H 5482 |
Chain | Residue |
G | HIS446 |
H | ILE15 |
H | GLY16 |
H | GLY18 |
H | PRO19 |
H | GLY20 |
H | GLU39 |
H | ALA40 |
H | GLU42 |
H | GLY45 |
H | CYS47 |
H | GLY51 |
H | CYS52 |
H | THR55 |
H | LYS56 |
H | GLY117 |
H | PHE118 |
H | ALA119 |
H | ALA146 |
H | THR147 |
H | GLY148 |
H | SER166 |
H | ARG274 |
H | ARG277 |
H | LEU281 |
H | GLY313 |
H | ASP314 |
H | LEU320 |
H | LEU321 |
H | ALA322 |
H | HIS323 |
H | TYR353 |
H | HOH5483 |
H | HOH5485 |
H | HOH5493 |
H | HOH5501 |
H | HOH5506 |
H | HOH5555 |
H | HOH5593 |
site_id | AC7 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE FAD J 6482 |
Chain | Residue |
J | ILE15 |
J | GLY16 |
J | GLY18 |
J | PRO19 |
J | GLY20 |
J | GLY21 |
J | GLU39 |
J | ALA40 |
J | GLU42 |
J | GLY45 |
J | CYS47 |
J | GLY51 |
J | CYS52 |
J | THR55 |
J | LYS56 |
J | GLY117 |
J | PHE118 |
J | ALA119 |
J | ALA146 |
J | THR147 |
J | GLY148 |
J | SER166 |
J | ARG274 |
J | LEU281 |
J | GLY313 |
J | ASP314 |
J | LEU320 |
J | LEU321 |
J | ALA322 |
J | HIS323 |
J | TYR353 |
J | HOH6495 |
J | HOH6496 |
J | HOH6516 |
J | HOH6524 |
J | HOH6528 |
K | HIS446 |
site_id | AC8 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD K 7482 |
Chain | Residue |
J | HIS446 |
K | ILE15 |
K | GLY16 |
K | GLY18 |
K | PRO19 |
K | GLY20 |
K | GLU39 |
K | ALA40 |
K | GLU42 |
K | GLY45 |
K | CYS47 |
K | GLY51 |
K | CYS52 |
K | THR55 |
K | LYS56 |
K | PHE118 |
K | ALA119 |
K | ALA146 |
K | THR147 |
K | GLY148 |
K | SER166 |
K | ARG274 |
K | ARG277 |
K | LEU281 |
K | GLY313 |
K | ASP314 |
K | LEU320 |
K | LEU321 |
K | ALA322 |
K | HIS323 |
K | TYR353 |
K | HOH7487 |
K | HOH7489 |
K | HOH7523 |
Functional Information from PROSITE/UniProt
site_id | PS00076 |
Number of Residues | 11 |
Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGvCLnvGCIP |
Chain | Residue | Details |
A | GLY44-PRO54 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
A | CYS47 | |
A | CYS52 |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
B | GLU451 | |
B | HIS446 |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
D | GLU451 | |
D | HIS446 |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
E | GLU451 | |
E | HIS446 |
site_id | CSA13 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
G | GLU451 | |
G | HIS446 |
site_id | CSA14 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
H | GLU451 | |
H | HIS446 |
site_id | CSA15 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
J | GLU451 | |
J | HIS446 |
site_id | CSA16 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
K | GLU451 | |
K | HIS446 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
B | CYS47 | |
B | CYS52 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
D | CYS47 | |
D | CYS52 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
E | CYS47 | |
E | CYS52 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
G | CYS47 | |
G | CYS52 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
H | CYS47 | |
H | CYS52 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
J | CYS47 | |
J | CYS52 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
K | CYS47 | |
K | CYS52 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
A | GLU451 | |
A | HIS446 |