3BG3
Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus)
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN A 2001 |
| Chain | Residue |
| A | ASP572 |
| A | HIS771 |
| A | HIS773 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN B 2001 |
| Chain | Residue |
| B | ASP572 |
| B | HIS771 |
| B | HIS773 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN C 2001 |
| Chain | Residue |
| C | ASP572 |
| C | HIS771 |
| C | HIS773 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN D 2001 |
| Chain | Residue |
| D | ASP572 |
| D | HIS771 |
| D | HIS773 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PYR A 2000 |
| Chain | Residue |
| A | ARG571 |
| A | GLN575 |
| A | GLY609 |
| A | LEU642 |
| A | ARG644 |
| A | THR908 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BTI A 2100 |
| Chain | Residue |
| A | LYS1144 |
| B | GLN575 |
| B | PHE618 |
| B | ARG644 |
| B | TYR651 |
| B | GLN870 |
| B | THR908 |
| B | SER911 |
| B | LYS912 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PYR B 2000 |
| Chain | Residue |
| B | ARG571 |
| B | ASP572 |
| B | GLN575 |
| B | GLY609 |
| B | LEU642 |
| B | ARG644 |
| B | THR908 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PYR C 2000 |
| Chain | Residue |
| C | ARG571 |
| C | GLN575 |
| C | LEU642 |
| C | ARG644 |
| C | THR908 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PYR D 2000 |
| Chain | Residue |
| D | ARG571 |
| D | GLN575 |
| D | GLY609 |
| D | LEU642 |
| D | ARG644 |
| D | THR908 |
Functional Information from PROSITE/UniProt
| site_id | PS00188 |
| Number of Residues | 18 |
| Details | BIOTIN Biotin-requiring enzymes attachment site. GQpLcvLsAMKMetvVtS |
| Chain | Residue | Details |
| A | GLY1134-SER1151 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18297087","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"18297087","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 34 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q05920","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"18297087","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P52873","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-biotinyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6548474","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7918683","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
