3NVL
Crystal Structure of Phosphoglycerate Mutase from Trypanosoma brucei
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004619 | molecular_function | phosphoglycerate mutase activity |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006007 | biological_process | glucose catabolic process |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046537 | molecular_function | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097014 | cellular_component | ciliary plasm |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004619 | molecular_function | phosphoglycerate mutase activity |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006007 | biological_process | glucose catabolic process |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046537 | molecular_function | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0097014 | cellular_component | ciliary plasm |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 552 |
| Chain | Residue |
| A | HIS135 |
| A | ARG165 |
| A | ARG201 |
| A | ARG281 |
| A | ARG284 |
| A | HOH693 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 553 |
| Chain | Residue |
| A | ASP465 |
| A | HIS466 |
| A | ASP22 |
| A | SER74 |
| A | LYS356 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 554 |
| Chain | Residue |
| A | ASP319 |
| A | ASP424 |
| A | HIS428 |
| A | HIS495 |
| A | HOH695 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 552 |
| Chain | Residue |
| B | HIS135 |
| B | ARG165 |
| B | ARG201 |
| B | ARG208 |
| B | ARG284 |
| B | HOH647 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO B 553 |
| Chain | Residue |
| B | ASP22 |
| B | SER74 |
| B | ASP465 |
| B | HIS466 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO B 554 |
| Chain | Residue |
| B | ASP319 |
| B | ASP424 |
| B | HIS428 |
| B | HIS495 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Phosphoserine intermediate => ECO:0000255|PIRSR:PIRSR001492-1, ECO:0000269|PubMed:11682175 |
| Chain | Residue | Details |
| A | SER74 | |
| B | SER74 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|PIRSR:PIRSR001492-3, ECO:0000305|PubMed:22458781, ECO:0007744|PDB:3NVL |
| Chain | Residue | Details |
| A | ASP22 | |
| B | ASP424 | |
| B | HIS428 | |
| B | ASP465 | |
| B | HIS466 | |
| B | HIS495 | |
| A | SER74 | |
| A | ASP424 | |
| A | HIS428 | |
| A | ASP465 | |
| A | HIS466 | |
| A | HIS495 | |
| B | ASP22 | |
| B | SER74 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|PIRSR:PIRSR001492-2 |
| Chain | Residue | Details |
| A | HIS135 | |
| B | ARG208 | |
| B | ARG281 | |
| B | LYS356 | |
| A | ARG165 | |
| A | ARG201 | |
| A | ARG208 | |
| A | ARG281 | |
| A | LYS356 | |
| B | HIS135 | |
| B | ARG165 | |
| B | ARG201 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:22458781, ECO:0007744|PDB:3NVL |
| Chain | Residue | Details |
| A | ASP319 | |
| B | ASP319 |
