2PC9
Crystal Structure Of ATP-Dependent Phosphoenolpyruvate Carboxykinase From Thermus thermophilus HB8
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004611 | molecular_function | phosphoenolpyruvate carboxykinase activity |
A | 0004612 | molecular_function | phosphoenolpyruvate carboxykinase (ATP) activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006094 | biological_process | gluconeogenesis |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0017076 | molecular_function | purine nucleotide binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0004611 | molecular_function | phosphoenolpyruvate carboxykinase activity |
B | 0004612 | molecular_function | phosphoenolpyruvate carboxykinase (ATP) activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006094 | biological_process | gluconeogenesis |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0017076 | molecular_function | purine nucleotide binding |
B | 0046872 | molecular_function | metal ion binding |
C | 0004611 | molecular_function | phosphoenolpyruvate carboxykinase activity |
C | 0004612 | molecular_function | phosphoenolpyruvate carboxykinase (ATP) activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006094 | biological_process | gluconeogenesis |
C | 0016831 | molecular_function | carboxy-lyase activity |
C | 0017076 | molecular_function | purine nucleotide binding |
C | 0046872 | molecular_function | metal ion binding |
D | 0004611 | molecular_function | phosphoenolpyruvate carboxykinase activity |
D | 0004612 | molecular_function | phosphoenolpyruvate carboxykinase (ATP) activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006094 | biological_process | gluconeogenesis |
D | 0016831 | molecular_function | carboxy-lyase activity |
D | 0017076 | molecular_function | purine nucleotide binding |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00532 |
Number of Residues | 16 |
Details | PEPCK_ATP Phosphoenolpyruvate carboxykinase (ATP) signature. LIGDDEHgWsEdGVfN |
Chain | Residue | Details |
A | LEU249-ASN264 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00453 |
Chain | Residue | Details |
A | ARG52 | |
B | ASP253 | |
B | GLU281 | |
B | ARG319 | |
C | ARG52 | |
C | TYR191 | |
C | LYS197 | |
C | ASP253 | |
C | GLU281 | |
C | ARG319 | |
D | ARG52 | |
A | TYR191 | |
D | TYR191 | |
D | LYS197 | |
D | ASP253 | |
D | GLU281 | |
D | ARG319 | |
A | LYS197 | |
A | ASP253 | |
A | GLU281 | |
A | ARG319 | |
B | ARG52 | |
B | TYR191 | |
B | LYS197 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9 |
Chain | Residue | Details |
A | ARG130 | |
D | ARG130 | |
D | ASN131 | |
D | GLY267 | |
A | ASN131 | |
A | GLY267 | |
B | ARG130 | |
B | ASN131 | |
B | GLY267 | |
C | ARG130 | |
C | ASN131 | |
C | GLY267 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:2PC9 |
Chain | Residue | Details |
A | PHE133 | |
B | PHE133 | |
C | PHE133 | |
D | PHE133 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P22259 |
Chain | Residue | Details |
A | HIS216 | |
B | HIS216 | |
C | HIS216 | |
D | HIS216 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9 |
Chain | Residue | Details |
A | GLY232 | |
A | THR444 | |
B | GLY232 | |
B | THR444 | |
C | GLY232 | |
C | THR444 | |
D | GLY232 | |
D | THR444 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:16239727, ECO:0000305|Ref.3, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9 |
Chain | Residue | Details |
A | ARG438 | |
B | ARG438 | |
C | ARG438 | |
D | ARG438 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3 |
Chain | Residue | Details |
A | PHE439 | |
B | PHE439 | |
C | PHE439 | |
D | PHE439 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1aq2 |
Chain | Residue | Details |
A | HIS216 | |
A | ARG319 | |
A | LYS238 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1aq2 |
Chain | Residue | Details |
B | HIS216 | |
B | ARG319 | |
B | LYS238 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1aq2 |
Chain | Residue | Details |
C | HIS216 | |
C | ARG319 | |
C | LYS238 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1aq2 |
Chain | Residue | Details |
D | HIS216 | |
D | ARG319 | |
D | LYS238 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1aq2 |
Chain | Residue | Details |
A | HIS216 | |
A | ARG319 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1aq2 |
Chain | Residue | Details |
B | HIS216 | |
B | ARG319 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1aq2 |
Chain | Residue | Details |
C | HIS216 | |
C | ARG319 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1aq2 |
Chain | Residue | Details |
D | HIS216 | |
D | ARG319 |