1OHY
4-AMINOBUTYRATE-AMINOTRANSFERASE inactivated by gamma-ethynyl GABA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005829 | cellular_component | cytosol |
A | 0008483 | molecular_function | transaminase activity |
A | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
A | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0032144 | cellular_component | 4-aminobutyrate transaminase complex |
A | 0032145 | molecular_function | succinate-semialdehyde dehydrogenase binding |
A | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0047298 | molecular_function | (S)-3-amino-2-methylpropionate transaminase activity |
A | 0050877 | biological_process | nervous system process |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0005829 | cellular_component | cytosol |
B | 0008483 | molecular_function | transaminase activity |
B | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
B | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
B | 0016740 | molecular_function | transferase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0032144 | cellular_component | 4-aminobutyrate transaminase complex |
B | 0032145 | molecular_function | succinate-semialdehyde dehydrogenase binding |
B | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0047298 | molecular_function | (S)-3-amino-2-methylpropionate transaminase activity |
B | 0050877 | biological_process | nervous system process |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
C | 0005739 | cellular_component | mitochondrion |
C | 0005759 | cellular_component | mitochondrial matrix |
C | 0005829 | cellular_component | cytosol |
C | 0008483 | molecular_function | transaminase activity |
C | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
C | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
C | 0016740 | molecular_function | transferase activity |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0032144 | cellular_component | 4-aminobutyrate transaminase complex |
C | 0032145 | molecular_function | succinate-semialdehyde dehydrogenase binding |
C | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0047298 | molecular_function | (S)-3-amino-2-methylpropionate transaminase activity |
C | 0050877 | biological_process | nervous system process |
C | 0051536 | molecular_function | iron-sulfur cluster binding |
C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
D | 0005739 | cellular_component | mitochondrion |
D | 0005759 | cellular_component | mitochondrial matrix |
D | 0005829 | cellular_component | cytosol |
D | 0008483 | molecular_function | transaminase activity |
D | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
D | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
D | 0016740 | molecular_function | transferase activity |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0032144 | cellular_component | 4-aminobutyrate transaminase complex |
D | 0032145 | molecular_function | succinate-semialdehyde dehydrogenase binding |
D | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0042803 | molecular_function | protein homodimerization activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0047298 | molecular_function | (S)-3-amino-2-methylpropionate transaminase activity |
D | 0050877 | biological_process | nervous system process |
D | 0051536 | molecular_function | iron-sulfur cluster binding |
D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FES A 800 |
Chain | Residue |
A | ALA134 |
A | CYS135 |
A | CYS138 |
B | ALA134 |
B | CYS135 |
B | CYS138 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FES C 800 |
Chain | Residue |
D | ALA134 |
D | CYS135 |
D | CYS138 |
C | ALA134 |
C | CYS135 |
C | CYS138 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PLP A 600 |
Chain | Residue |
A | GLY136 |
A | SER137 |
A | ASN140 |
A | PHE189 |
A | HIS190 |
A | GLY191 |
A | GLU265 |
A | ASP298 |
A | VAL300 |
A | GLN301 |
A | LYS329 |
A | GEG700 |
A | HOH2059 |
A | HOH2060 |
B | THR353 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GEG A 700 |
Chain | Residue |
A | ILE72 |
A | PHE189 |
A | ARG192 |
A | LYS329 |
A | PLP600 |
B | PHE351 |
B | ASN352 |
B | THR353 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PLP B 600 |
Chain | Residue |
A | THR353 |
B | GLY136 |
B | SER137 |
B | ASN140 |
B | PHE189 |
B | HIS190 |
B | GLY191 |
B | GLU265 |
B | ASP298 |
B | VAL300 |
B | GLN301 |
B | LYS329 |
B | GEG700 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GEG B 700 |
Chain | Residue |
A | PHE351 |
A | THR353 |
B | ILE72 |
B | PHE189 |
B | ARG192 |
B | LYS329 |
B | PLP600 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP C 600 |
Chain | Residue |
C | GLY136 |
C | SER137 |
C | ASN140 |
C | PHE189 |
C | HIS190 |
C | GLY191 |
C | GLU265 |
C | ASP298 |
C | VAL300 |
C | GLN301 |
C | LYS329 |
C | GEG700 |
C | HOH2091 |
D | THR353 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GEG C 700 |
Chain | Residue |
C | ILE72 |
C | PHE189 |
C | ARG192 |
C | LYS329 |
C | PLP600 |
D | PHE351 |
D | THR353 |
site_id | AC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PLP D 600 |
Chain | Residue |
C | THR353 |
D | GLY136 |
D | SER137 |
D | ASN140 |
D | PHE189 |
D | HIS190 |
D | GLY191 |
D | GLU265 |
D | ASP298 |
D | VAL300 |
D | GLN301 |
D | LYS329 |
D | GEG700 |
D | HOH2050 |
D | HOH2078 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GEG D 700 |
Chain | Residue |
D | HOH2078 |
C | PHE351 |
C | THR353 |
D | ILE72 |
D | PHE189 |
D | ARG192 |
D | GLU270 |
D | LYS329 |
D | PLP600 |
Functional Information from PROSITE/UniProt
site_id | PS00600 |
Number of Residues | 40 |
Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FLvDEVqtgGG.StGkfwahehwglddpa..DVMtfSKkmmTG |
Chain | Residue | Details |
A | PHE295-GLY334 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"14534310","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"10393538","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"14534310","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10393538","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10393538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14534310","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P61922","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P61922","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 16 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P61922","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10393538","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
A | ASP298 | |
A | PHE189 | |
A | LYS329 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
B | ASP298 | |
B | PHE189 | |
B | LYS329 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
C | ASP298 | |
C | PHE189 | |
C | LYS329 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
D | ASP298 | |
D | PHE189 | |
D | LYS329 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 854 |
Chain | Residue | Details |
A | PHE189 | steric role |
A | ASP298 | electrostatic stabiliser |
A | LYS329 | covalent catalysis, proton shuttle (general acid/base) |
A | THR353 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 854 |
Chain | Residue | Details |
B | PHE189 | steric role |
B | ASP298 | electrostatic stabiliser |
B | LYS329 | covalent catalysis, proton shuttle (general acid/base) |
B | THR353 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 854 |
Chain | Residue | Details |
C | PHE189 | steric role |
C | ASP298 | electrostatic stabiliser |
C | LYS329 | covalent catalysis, proton shuttle (general acid/base) |
C | THR353 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 854 |
Chain | Residue | Details |
D | PHE189 | steric role |
D | ASP298 | electrostatic stabiliser |
D | LYS329 | covalent catalysis, proton shuttle (general acid/base) |
D | THR353 | electrostatic stabiliser |