5KVU
Crystal structure of isocitrate dehydrogenase-2 in complex with NADP(+) from Mycobacterium tuberculosis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
A | 0005576 | cellular_component | extracellular region |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006097 | biological_process | glyoxylate cycle |
A | 0006099 | biological_process | tricarboxylic acid cycle |
A | 0006102 | biological_process | isocitrate metabolic process |
A | 0009274 | cellular_component | peptidoglycan-based cell wall |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006097 | biological_process | glyoxylate cycle |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0006102 | biological_process | isocitrate metabolic process |
B | 0009274 | cellular_component | peptidoglycan-based cell wall |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
C | 0005576 | cellular_component | extracellular region |
C | 0005829 | cellular_component | cytosol |
C | 0005886 | cellular_component | plasma membrane |
C | 0006097 | biological_process | glyoxylate cycle |
C | 0006099 | biological_process | tricarboxylic acid cycle |
C | 0006102 | biological_process | isocitrate metabolic process |
C | 0009274 | cellular_component | peptidoglycan-based cell wall |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
D | 0005576 | cellular_component | extracellular region |
D | 0005829 | cellular_component | cytosol |
D | 0005886 | cellular_component | plasma membrane |
D | 0006097 | biological_process | glyoxylate cycle |
D | 0006099 | biological_process | tricarboxylic acid cycle |
D | 0006102 | biological_process | isocitrate metabolic process |
D | 0009274 | cellular_component | peptidoglycan-based cell wall |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0042803 | molecular_function | protein homodimerization activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | binding site for residue NAP A 801 |
Chain | Residue |
A | LYS84 |
A | ALA566 |
A | GLY586 |
A | GLY587 |
A | SER588 |
A | ALA589 |
A | PRO590 |
A | HIS592 |
A | ARG603 |
A | TRP604 |
A | ASP605 |
A | PRO86 |
A | ARG652 |
A | MLT802 |
A | HOH935 |
A | HOH943 |
A | HOH954 |
A | HOH978 |
A | ASN87 |
A | SER89 |
A | ASN137 |
A | ARG141 |
A | ILE350 |
A | ALA353 |
A | THR564 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue MLT A 802 |
Chain | Residue |
A | SER89 |
A | SER134 |
A | ASN137 |
A | ARG141 |
A | TYR422 |
A | ARG550 |
A | ASP551 |
A | NAP801 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue EDO A 803 |
Chain | Residue |
A | ARG526 |
A | ARG529 |
A | GLU533 |
site_id | AC4 |
Number of Residues | 22 |
Details | binding site for residue NAP B 801 |
Chain | Residue |
B | LYS84 |
B | PRO86 |
B | ASN87 |
B | SER89 |
B | ASN137 |
B | ILE350 |
B | ALA353 |
B | THR564 |
B | ALA566 |
B | GLY586 |
B | GLY587 |
B | SER588 |
B | ALA589 |
B | PRO590 |
B | HIS592 |
B | ARG603 |
B | TRP604 |
B | ASP605 |
B | ARG652 |
B | MLA802 |
B | HOH904 |
B | HOH949 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue MLA B 802 |
Chain | Residue |
B | SER89 |
B | SER134 |
B | ASN137 |
B | ARG141 |
B | LYS257 |
B | TYR422 |
B | ARG550 |
B | ASP551 |
B | NAP801 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue EDO B 803 |
Chain | Residue |
B | ILE502 |
B | LYS506 |
B | ILE521 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO B 804 |
Chain | Residue |
B | MET522 |
B | SER523 |
B | ARG526 |
B | HOH905 |
site_id | AC8 |
Number of Residues | 26 |
Details | binding site for residue NAP C 801 |
Chain | Residue |
C | HOH961 |
C | LYS84 |
C | PRO86 |
C | ASN87 |
C | ILE88 |
C | SER89 |
C | ASN137 |
C | ARG141 |
C | ILE350 |
C | ALA353 |
C | THR564 |
C | ALA566 |
C | GLY586 |
C | GLY587 |
C | SER588 |
C | ALA589 |
C | PRO590 |
C | HIS592 |
C | ARG603 |
C | TRP604 |
C | ASP605 |
C | SIN802 |
C | HOH918 |
C | HOH931 |
C | HOH940 |
C | HOH958 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue SIN C 802 |
Chain | Residue |
C | SER89 |
C | ASN137 |
C | ARG141 |
C | LYS257 |
C | TYR422 |
C | ARG550 |
C | ASP551 |
C | NAP801 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue GOL C 803 |
Chain | Residue |
C | VAL334 |
C | ASP335 |
C | SER336 |
C | TYR366 |
C | LYS591 |
C | HOH930 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue EDO C 804 |
Chain | Residue |
C | GLY484 |
C | MET485 |
C | ASP540 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue EDO C 805 |
Chain | Residue |
C | THR191 |
C | GLU500 |
C | LYS503 |
C | LYS504 |
C | THR507 |
site_id | AD4 |
Number of Residues | 30 |
Details | binding site for residue NAP D 801 |
Chain | Residue |
D | LYS84 |
D | PRO86 |
D | ASN87 |
D | ILE88 |
D | SER89 |
D | ASN137 |
D | ARG141 |
D | ILE350 |
D | ALA353 |
D | THR564 |
D | ALA566 |
D | GLY586 |
D | GLY587 |
D | SER588 |
D | ALA589 |
D | PRO590 |
D | LYS591 |
D | HIS592 |
D | ARG603 |
D | TRP604 |
D | ASP605 |
D | ARG652 |
D | MLA802 |
D | EDO804 |
D | HOH919 |
D | HOH920 |
D | HOH928 |
D | HOH938 |
D | HOH943 |
D | HOH958 |
site_id | AD5 |
Number of Residues | 9 |
Details | binding site for residue MLA D 802 |
Chain | Residue |
D | SER89 |
D | SER134 |
D | ASN137 |
D | ARG141 |
D | LYS257 |
D | TYR422 |
D | ARG550 |
D | ASP551 |
D | NAP801 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue GOL D 803 |
Chain | Residue |
D | VAL334 |
D | SER336 |
D | TYR366 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue EDO D 804 |
Chain | Residue |
D | ILE559 |
D | GLY563 |
D | THR564 |
D | SER565 |
D | NAP801 |
D | HOH943 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 36 |
Details | BINDING: BINDING => ECO:0000269|Ref.5, ECO:0007744|PDB:5KVU |
Chain | Residue | Details |
A | ASN87 | |
B | ASN87 | |
B | SER89 | |
B | GLY587 | |
B | SER588 | |
B | ALA589 | |
B | HIS592 | |
B | ARG603 | |
B | ASP605 | |
B | ARG652 | |
C | ASN87 | |
A | SER89 | |
C | SER89 | |
C | GLY587 | |
C | SER588 | |
C | ALA589 | |
C | HIS592 | |
C | ARG603 | |
C | ASP605 | |
C | ARG652 | |
D | ASN87 | |
D | SER89 | |
A | GLY587 | |
D | GLY587 | |
D | SER588 | |
D | ALA589 | |
D | HIS592 | |
D | ARG603 | |
D | ASP605 | |
D | ARG652 | |
A | SER588 | |
A | ALA589 | |
A | HIS592 | |
A | ARG603 | |
A | ASP605 | |
A | ARG652 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000305|Ref.5, ECO:0007744|PDB:5KVU |
Chain | Residue | Details |
A | SER134 | |
B | LYS257 | |
B | TYR422 | |
B | ARG550 | |
C | SER134 | |
C | ASN137 | |
C | ARG141 | |
C | LYS257 | |
C | TYR422 | |
C | ARG550 | |
D | SER134 | |
A | ASN137 | |
D | ASN137 | |
D | ARG141 | |
D | LYS257 | |
D | TYR422 | |
D | ARG550 | |
A | ARG141 | |
A | LYS257 | |
A | TYR422 | |
A | ARG550 | |
B | SER134 | |
B | ASN137 | |
B | ARG141 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P16100 |
Chain | Residue | Details |
A | ARG147 | |
B | ARG147 | |
C | ARG147 | |
D | ARG147 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P50216 |
Chain | Residue | Details |
A | ASP352 | |
D | ASP352 | |
D | ASP551 | |
D | ASP555 | |
A | ASP551 | |
A | ASP555 | |
B | ASP352 | |
B | ASP551 | |
B | ASP555 | |
C | ASP352 | |
C | ASP551 | |
C | ASP555 |