4TYQ
Crystal structure of an adenylate kinase mutant--AKm2
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B | Adenylate kinase | polymer | 217 | 24406.1 | 2 | UniProt (P16304) Pfam (PF00406) Pfam (PF05191) In PDB | Bacillus subtilis 168 | AK,ATP-AMP transphosphorylase,ATP:AMP phosphotransferase,Adenylate monophosphate kinase,Superoxide-inducible protein 16,SOI16 |
2 | A, B | BIS(ADENOSINE)-5'-PENTAPHOSPHATE | non-polymer | 916.4 | 2 | Chemie (AP5) | |||
3 | A, B | MAGNESIUM ION | non-polymer | 24.3 | 2 | Chemie (MG) | |||
4 | A, B | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
5 | A | CALCIUM ION | non-polymer | 40.1 | 1 | Chemie (CA) | |||
6 | water | water | 18.0 | 332 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 217 (UniProt: P16304)
PDB | External Database | Details |
---|---|---|
Ile 3 | Leu 3 | engineered mutation |
Ala 17 | Gly 17 | engineered mutation |
Ala 22 | Glu 22 | engineered mutation |
Lys 23 | Asp 23 | engineered mutation |
Arg 69 | Lys 69 | engineered mutation |
Ser 73 | Gly 73 | engineered mutation |
Ser 75 | Asp 75 | engineered mutation |
Met 103 | Tyr 103 | engineered mutation |
Arg 105 | Lys 105 | engineered mutation |
Lys 106 | Pro 106 | engineered mutation |
Leu 107 | Ile 107 | engineered mutation |
Glu 108 | Asp 108 | engineered mutation |
His 112 | Asn 112 | engineered mutation |
Arg 116 | Asp 116 | engineered mutation |
Gln 117 | Lys 117 | engineered mutation |
Glu 118 | Asp 118 | engineered mutation |
Glu 119 | Val 119 | engineered mutation |
Ala 169 | Ser 169 | engineered mutation |
Met 179 | Thr 179 | engineered mutation |
Ala 180 | Gln 180 | engineered mutation |
Ala 184 | Asp 184 | engineered mutation |
Asp 187 | Ser 187 | engineered mutation |
Ser 188 | Glu 188 | engineered mutation |
Glu 190 | Gly 190 | engineered mutation |
Val 191 | Tyr 191 | engineered mutation |
Val 193 | Ala 193 | engineered mutation |
Met 201 | Ile 201 | engineered mutation |
Glu 202 | Gln 202 | engineered mutation |
Lys 203 | Asp 203 | engineered mutation |
Phe 205 | Tyr 205 | engineered mutation |
Lys 206 | Ala 206 | engineered mutation |
Leu 208 | Val 208 | engineered mutation |
Arg 209 | Lys 209 | engineered mutation |
Glu 210 | Asp 210 | engineered mutation |
Ile 211 | Leu 211 | engineered mutation |
Gln 213 | Gly 213 | engineered mutation |
Ala 216 | Lys 216 | engineered mutation |
Arg 217 | Lys 217 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 48812.2 | |
Non-Polymers* | Number of molecules | 7 |
Total formula weight | 2052.2 | |
All* | Total formula weight | 50864.4 |