1ZUN
Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A | Sulfate adenylyltransferase subunit 2 | polymer | 325 | 37913.9 | 1 | UniProt (Q87WW0) Pfam (PF01507) In PDB | Pseudomonas syringae | Sulfate adenylate transferase, SAT, ATP-sulfurylase small subunit, ATP sulfurylase catalytic subunit (CysD) |
| 2 | B | sulfate adenylate transferase, subunit 1/adenylylsulfate kinase | polymer | 434 | 48304.8 | 1 | GenBank (28871567) Pfam (PF00009) Pfam (PF03144) UniProt (by SIFTS) (Q87WW1) In PDB | Pseudomonas syringae pv. tomato str. DC3000 | GTPase domain of ATP sulfurylase regulatory subunit (CysN) |
| 3 | A | MAGNESIUM ION | non-polymer | 24.3 | 1 | Chemie (MG) | |||
| 4 | A | SODIUM ION | non-polymer | 23.0 | 1 | Chemie (NA) | |||
| 5 | A | PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER | non-polymer | 523.2 | 1 | Chemie (AGS) | |||
| 6 | B | GUANOSINE-5'-DIPHOSPHATE | non-polymer | 443.2 | 1 | Chemie (GDP) | |||
| 7 | water | water | 18.0 | 87 | Chemie (HOH) |
Sequence modifications
A: -19 - 305 (UniProt: Q87WW0)
B: 1 - 434 (GenBank: 28871567)
| PDB | External Database | Details |
|---|---|---|
| Gly -18 | - | CLONING ARTIFACT |
| Ser -17 | - | CLONING ARTIFACT |
| Ser -16 | - | CLONING ARTIFACT |
| His -15 | - | CLONING ARTIFACT |
| His -14 | - | CLONING ARTIFACT |
| His -13 | - | CLONING ARTIFACT |
| His -12 | - | CLONING ARTIFACT |
| His -11 | - | CLONING ARTIFACT |
| His -10 | - | CLONING ARTIFACT |
| Ser -9 | - | CLONING ARTIFACT |
| Ser -8 | - | CLONING ARTIFACT |
| Gly -7 | - | CLONING ARTIFACT |
| Leu -6 | - | CLONING ARTIFACT |
| Val -5 | - | CLONING ARTIFACT |
| Pro -4 | - | CLONING ARTIFACT |
| Arg -3 | - | CLONING ARTIFACT |
| Gly -2 | - | CLONING ARTIFACT |
| Ser -1 | - | CLONING ARTIFACT |
| His 0 | - | CLONING ARTIFACT |
| Mse 1 | Met 1 | MODIFIED RESIDUE |
| Mse 31 | Met 31 | MODIFIED RESIDUE |
| Mse 42 | Met 42 | MODIFIED RESIDUE |
| Mse 60 | Met 60 | MODIFIED RESIDUE |
| Mse 71 | Met 71 | MODIFIED RESIDUE |
| Mse 78 | Met 78 | MODIFIED RESIDUE |
| Mse 82 | Met 82 | MODIFIED RESIDUE |
| Mse 113 | Met 113 | MODIFIED RESIDUE |
| PDB | External Database | Details |
|---|---|---|
| Mse 24 | Met 24 | MODIFIED RESIDUE |
| Mse 50 | Met 50 | MODIFIED RESIDUE |
| Mse 121 | Met 121 | MODIFIED RESIDUE |
| Mse 167 | Met 167 | MODIFIED RESIDUE |
| Mse 198 | Met 198 | MODIFIED RESIDUE |
| Mse 203 | Met 203 | MODIFIED RESIDUE |
| Mse 227 | Met 227 | MODIFIED RESIDUE |
| Mse 310 | Met 310 | MODIFIED RESIDUE |
| Mse 338 | Met 338 | MODIFIED RESIDUE |
| Mse 342 | Met 342 | MODIFIED RESIDUE |
| Mse 347 | Met 347 | MODIFIED RESIDUE |
| Mse 431 | Met 431 | MODIFIED RESIDUE |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 86218.6 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 1013.7 | |
| All* | Total formula weight | 87232.4 |
