4A0H
Structure of bifunctional DAPA aminotransferase-DTB synthetase from Arabidopsis thaliana bound to 7-keto 8-amino pelargonic acid (KAPA)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
A | 0004141 | molecular_function | dethiobiotin synthase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0008483 | molecular_function | transaminase activity |
A | 0009102 | biological_process | biotin biosynthetic process |
A | 0016874 | molecular_function | ligase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
B | 0004141 | molecular_function | dethiobiotin synthase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0008483 | molecular_function | transaminase activity |
B | 0009102 | biological_process | biotin biosynthetic process |
B | 0016874 | molecular_function | ligase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE KAP A 1808 |
Chain | Residue |
A | PHE326 |
A | PLP1644 |
B | GLY678 |
B | HIS679 |
B | SER680 |
A | TRP369 |
A | TRP370 |
A | TYR473 |
A | ALA587 |
A | LYS644 |
A | ARG775 |
A | PRO776 |
A | LEU777 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE KAP B 1808 |
Chain | Residue |
A | GLY678 |
B | TRP369 |
B | TRP370 |
B | TYR473 |
B | ALA587 |
B | LYS644 |
B | ARG775 |
B | PRO776 |
B | PLP1644 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE KAP A 1809 |
Chain | Residue |
A | GLY223 |
A | ILE225 |
A | SER226 |
B | THR24 |
B | THR59 |
B | SER143 |
B | SER195 |
B | TLA1810 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE KAP B 1809 |
Chain | Residue |
A | THR24 |
A | THR59 |
A | ALA141 |
A | ILE142 |
A | SER195 |
A | TLA1810 |
B | LEU222 |
B | GLY223 |
B | GLY224 |
B | ILE225 |
B | SER226 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TLA A 1810 |
Chain | Residue |
A | ASN23 |
A | THR24 |
A | SER25 |
A | LYS28 |
A | LYS55 |
A | ASP66 |
A | THR189 |
A | ALA190 |
A | GLY191 |
B | KAP1809 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TLA B 1810 |
Chain | Residue |
A | KAP1809 |
B | ASN23 |
B | THR24 |
B | SER25 |
B | LYS28 |
B | LYS55 |
B | ASP66 |
B | GLU188 |
B | GLY191 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP A 1644 |
Chain | Residue |
A | TRP370 |
A | ASN430 |
A | GLY431 |
A | SER432 |
A | TYR473 |
A | HIS474 |
A | GLU581 |
A | ASP615 |
A | VAL617 |
A | PHE618 |
A | LYS644 |
A | KAP1808 |
B | HIS679 |
B | SER680 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP B 1644 |
Chain | Residue |
A | HIS679 |
A | SER680 |
B | TRP370 |
B | ASN430 |
B | GLY431 |
B | SER432 |
B | TYR473 |
B | HIS474 |
B | GLU581 |
B | ASP615 |
B | VAL617 |
B | PHE618 |
B | LYS644 |
B | KAP1808 |
Functional Information from PROSITE/UniProt
site_id | PS00600 |
Number of Residues | 38 |
Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. VIfDEVft.GFwRlGvetttellgckp....DIAcfAKlltGG |
Chain | Residue | Details |
A | VAL612-GLY649 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P13000 |
Chain | Residue | Details |
A | SER25 | |
B | GLU523 | |
A | ASP75 | |
A | GLU248 | |
A | PRO496 | |
A | GLU523 | |
B | SER25 | |
B | ASP75 | |
B | GLU248 | |
B | PRO496 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0G |
Chain | Residue | Details |
A | THR29 | |
A | ASP66 | |
A | GLU188 | |
B | THR29 | |
B | ASP66 | |
B | GLU188 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0R |
Chain | Residue | Details |
A | THR59 | |
B | THR59 |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0H |
Chain | Residue | Details |
A | TRP369 | |
B | ARG775 | |
A | TYR473 | |
A | LYS644 | |
A | GLY678 | |
A | ARG775 | |
B | TRP369 | |
B | TYR473 | |
B | LYS644 | |
B | GLY678 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0G, ECO:0007744|PDB:4A0H, ECO:0007744|PDB:4A0R |
Chain | Residue | Details |
A | GLY431 | |
A | ASP615 | |
A | HIS679 | |
B | GLY431 | |
B | ASP615 | |
B | HIS679 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM => ECO:0000250|UniProtKB:P12995 |
Chain | Residue | Details |
A | PHE326 | |
B | PHE326 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0F, ECO:0007744|PDB:4A0G, ECO:0007744|PDB:4A0H, ECO:0007744|PDB:4A0R |
Chain | Residue | Details |
A | LYS644 | |
B | LYS644 |