1ZYL
Crystal Structure of Hypothetical Protein YihE from Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0006950 | biological_process | response to stress |
| A | 0016310 | biological_process | phosphorylation |
| A | 0044024 | molecular_function | histone H2AS1 kinase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01497, ECO:0000305|PubMed:17302814 |
| Chain | Residue | Details |
| A | ASP201 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01497, ECO:0000305|PubMed:17302814 |
| Chain | Residue | Details |
| A | ASP217 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01497, ECO:0000305|PubMed:17302814 |
| Chain | Residue | Details |
| A | ASN206 | |
| A | ASP217 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | SITE: ATP => ECO:0000255|HAMAP-Rule:MF_01497, ECO:0000305|PubMed:17302814 |
| Chain | Residue | Details |
| A | SER36 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1l8t |
| Chain | Residue | Details |
| A | ASP201 | |
| A | LYS55 |
