3R9A
Human alanine-glyoxylate aminotransferase in complex with the TPR domain of human PEX5P
Replaces: 3IMZFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004760 | molecular_function | L-serine-pyruvate transaminase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005782 | cellular_component | peroxisomal matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006563 | biological_process | L-serine metabolic process |
| A | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009436 | biological_process | glyoxylate catabolic process |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| A | 0019448 | biological_process | L-cysteine catabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042853 | biological_process | L-alanine catabolic process |
| A | 0046487 | biological_process | glyoxylate metabolic process |
| C | 0004760 | molecular_function | L-serine-pyruvate transaminase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005777 | cellular_component | peroxisome |
| C | 0005782 | cellular_component | peroxisomal matrix |
| C | 0005829 | cellular_component | cytosol |
| C | 0006563 | biological_process | L-serine metabolic process |
| C | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009436 | biological_process | glyoxylate catabolic process |
| C | 0016597 | molecular_function | amino acid binding |
| C | 0016740 | molecular_function | transferase activity |
| C | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| C | 0019448 | biological_process | L-cysteine catabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0042853 | biological_process | L-alanine catabolic process |
| C | 0046487 | biological_process | glyoxylate metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BTB C 393 |
| Chain | Residue |
| C | TRP246 |
| C | ASN249 |
| C | MET259 |
Functional Information from PROSITE/UniProt
| site_id | PS00595 |
| Number of Residues | 21 |
| Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDILysGSQKalnappGtSlI |
| Chain | Residue | Details |
| A | ILE200-ILE220 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"O35423","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O35423","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"28724525","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"24662292","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
