7BSL
Crystal Structure of human ME2 R67A mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004470 | molecular_function | malic enzyme activity |
A | 0004471 | molecular_function | malate dehydrogenase (decarboxylating) (NAD+) activity |
A | 0004473 | molecular_function | malate dehydrogenase (decarboxylating) (NADP+) activity |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0006090 | biological_process | pyruvate metabolic process |
A | 0006108 | biological_process | malate metabolic process |
A | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
A | 0009055 | molecular_function | electron transfer activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
A | 0046872 | molecular_function | metal ion binding |
A | 0051287 | molecular_function | NAD binding |
A | 1902031 | biological_process | regulation of NADP metabolic process |
B | 0004470 | molecular_function | malic enzyme activity |
B | 0004471 | molecular_function | malate dehydrogenase (decarboxylating) (NAD+) activity |
B | 0004473 | molecular_function | malate dehydrogenase (decarboxylating) (NADP+) activity |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0006090 | biological_process | pyruvate metabolic process |
B | 0006108 | biological_process | malate metabolic process |
B | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
B | 0009055 | molecular_function | electron transfer activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
B | 0046872 | molecular_function | metal ion binding |
B | 0051287 | molecular_function | NAD binding |
B | 1902031 | biological_process | regulation of NADP metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | binding site for residue NAD A 601 |
Chain | Residue |
A | ASN259 |
A | ALA393 |
A | GLY394 |
A | ALA395 |
A | LEU398 |
A | LEU419 |
A | SER420 |
A | ASN421 |
A | PRO422 |
A | GLN425 |
A | ASN467 |
A | ASP279 |
A | THR283 |
A | GLY311 |
A | ALA312 |
A | GLY313 |
A | ASP345 |
A | LYS346 |
A | VAL392 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue NAD A 602 |
Chain | Residue |
A | LYS156 |
A | GLY192 |
A | ILE193 |
A | ARG194 |
A | ARG197 |
A | ILE479 |
A | LEU480 |
A | ASN482 |
A | ARG542 |
A | TYR552 |
A | GLU555 |
A | ARG556 |
A | TRP558 |
site_id | AC3 |
Number of Residues | 18 |
Details | binding site for residue NAD B 601 |
Chain | Residue |
A | LYS453 |
A | GLY457 |
B | ARG165 |
B | LEU167 |
B | ASN259 |
B | PHE263 |
B | GLY311 |
B | ALA312 |
B | GLY313 |
B | ASP345 |
B | LYS346 |
B | VAL392 |
B | ALA393 |
B | GLY394 |
B | LEU398 |
B | SER420 |
B | ASN421 |
B | PRO422 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue NAD B 602 |
Chain | Residue |
A | ARG245 |
B | LYS156 |
B | GLY192 |
B | ILE193 |
B | ARG194 |
B | ILE479 |
B | LEU480 |
B | ASN482 |
B | ARG542 |
B | ARG556 |
B | TRP558 |
Functional Information from PROSITE/UniProt
site_id | PS00331 |
Number of Residues | 17 |
Details | MALIC_ENZYMES Malic enzymes signature. FnDDiqGTAaVaLAGLL |
Chain | Residue | Details |
A | PHE276-LEU292 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:12962632 |
Chain | Residue | Details |
A | TYR112 | |
B | TYR112 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:12962632 |
Chain | Residue | Details |
A | LYS183 | |
B | LYS183 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12121650, ECO:0000269|PubMed:12962632, ECO:0007744|PDB:1GZ3, ECO:0007744|PDB:1GZ4, ECO:0007744|PDB:1PJ2, ECO:0007744|PDB:1PJ3, ECO:0007744|PDB:1PJ4 |
Chain | Residue | Details |
A | ALA67 | |
A | ARG91 | |
B | ALA67 | |
B | ARG91 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10700286, ECO:0000269|PubMed:12962632, ECO:0007744|PDB:1DO8, ECO:0007744|PDB:1EFK, ECO:0007744|PDB:1EFL, ECO:0007744|PDB:1PJ3, ECO:0007744|PDB:1PJL, ECO:0007744|PDB:1QR6 |
Chain | Residue | Details |
A | ARG165 | |
A | ALA312 | |
B | ARG165 | |
B | ALA312 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10700286, ECO:0000269|PubMed:12121650, ECO:0000269|PubMed:12962632, ECO:0007744|PDB:1DO8, ECO:0007744|PDB:1EFK, ECO:0007744|PDB:1EFL, ECO:0007744|PDB:1GZ3, ECO:0007744|PDB:1GZ4, ECO:0007744|PDB:1PJ2, ECO:0007744|PDB:1PJ3, ECO:0007744|PDB:1PJ4 |
Chain | Residue | Details |
A | GLU255 | |
A | ASP256 | |
A | ASP279 | |
B | GLU255 | |
B | ASP256 | |
B | ASP279 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10700286, ECO:0000269|PubMed:12962632, ECO:0007744|PDB:1DO8, ECO:0007744|PDB:1EFK, ECO:0007744|PDB:1EFL, ECO:0007744|PDB:1PJ3, ECO:0007744|PDB:1QR6 |
Chain | Residue | Details |
A | ASN259 | |
B | ASN259 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0007744|PDB:1DO8, ECO:0007744|PDB:1EFK, ECO:0007744|PDB:1EFL, ECO:0007744|PDB:1PJ3, ECO:0007744|PDB:1QR6 |
Chain | Residue | Details |
A | GLU314 | |
B | GLU314 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0007744|PDB:1DO8, ECO:0007744|PDB:1EFK, ECO:0007744|PDB:1EFL, ECO:0007744|PDB:1PJ3, ECO:0007744|PDB:1PJL, ECO:0007744|PDB:1QR6 |
Chain | Residue | Details |
A | ALA315 | |
B | ALA315 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12962632, ECO:0007744|PDB:1PJ2, ECO:0007744|PDB:1PJ4 |
Chain | Residue | Details |
A | ASN421 | |
A | ASN466 | |
B | ASN421 | |
B | ASN466 |
site_id | SWS_FT_FI10 |
Number of Residues | 10 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS156 | |
B | LYS346 | |
A | LYS224 | |
A | LYS240 | |
A | LYS272 | |
A | LYS346 | |
B | LYS156 | |
B | LYS224 | |
B | LYS240 | |
B | LYS272 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 21 |
Chain | Residue | Details |
A | TYR112 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ARG165 | electrostatic stabiliser, hydrogen bond donor |
A | LYS183 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | GLU255 | metal ligand |
A | ASP256 | metal ligand |
A | ASP278 | hydrogen bond acceptor, proton acceptor, proton donor |
A | ASP279 | metal ligand |
A | ASN421 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 8 |
Details | M-CSA 21 |
Chain | Residue | Details |
B | TYR112 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | ARG165 | electrostatic stabiliser, hydrogen bond donor |
B | LYS183 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | GLU255 | metal ligand |
B | ASP256 | metal ligand |
B | ASP278 | hydrogen bond acceptor, proton acceptor, proton donor |
B | ASP279 | metal ligand |
B | ASN421 | electrostatic stabiliser, hydrogen bond donor |