2YCB
Structure of the archaeal beta-CASP protein with N-terminal KH domains from Methanothermobacter thermautotrophicus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0004521 | molecular_function | RNA endonuclease activity |
| A | 0004527 | molecular_function | exonuclease activity |
| A | 0004532 | molecular_function | RNA exonuclease activity |
| A | 0004540 | molecular_function | RNA nuclease activity |
| A | 0006353 | biological_process | DNA-templated transcription termination |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0004521 | molecular_function | RNA endonuclease activity |
| B | 0004527 | molecular_function | exonuclease activity |
| B | 0004532 | molecular_function | RNA exonuclease activity |
| B | 0004540 | molecular_function | RNA nuclease activity |
| B | 0006353 | biological_process | DNA-templated transcription termination |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 1637 |
| Chain | Residue |
| A | ASP246 |
| A | HIS247 |
| A | ASP352 |
| A | HIS603 |
| A | ZN1638 |
| A | PO41639 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 1638 |
| Chain | Residue |
| A | ASP352 |
| A | ZN1637 |
| A | PO41639 |
| A | HIS242 |
| A | HIS244 |
| A | HIS329 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1639 |
| Chain | Residue |
| A | HIS242 |
| A | HIS244 |
| A | ASP246 |
| A | HIS247 |
| A | HIS329 |
| A | ASP352 |
| A | HIS579 |
| A | HIS603 |
| A | ZN1637 |
| A | ZN1638 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1640 |
| Chain | Residue |
| A | ARG135 |
| A | ARG467 |
| A | ASP468 |
| A | HIS472 |
| A | PO41641 |
| A | ZN1642 |
| B | HIS472 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1641 |
| Chain | Residue |
| A | LYS464 |
| A | ARG467 |
| A | ASP468 |
| A | PO41640 |
| A | ZN1642 |
| B | HIS472 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1642 |
| Chain | Residue |
| A | ASP468 |
| A | HIS472 |
| A | PO41640 |
| A | PO41641 |
| B | HIS472 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K A 1643 |
| Chain | Residue |
| A | LEU225 |
| A | VAL227 |
| A | PHE230 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 1637 |
| Chain | Residue |
| B | ASP246 |
| B | HIS247 |
| B | ASP352 |
| B | HIS603 |
| B | ZN1638 |
| B | PO41639 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 1638 |
| Chain | Residue |
| B | HIS242 |
| B | HIS244 |
| B | HIS329 |
| B | ASP352 |
| B | ZN1637 |
| B | PO41639 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1639 |
| Chain | Residue |
| B | HIS242 |
| B | HIS244 |
| B | ASP246 |
| B | HIS247 |
| B | HIS329 |
| B | ASP352 |
| B | HIS579 |
| B | HIS603 |
| B | ZN1637 |
| B | ZN1638 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K B 1640 |
| Chain | Residue |
| B | LEU225 |
| B | VAL227 |
| B | PHE230 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 134 |
| Details | Region: {"description":"KHa","evidences":[{"source":"HAMAP-Rule","id":"MF_00870","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21565697","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 134 |
| Details | Region: {"description":"KHb","evidences":[{"source":"HAMAP-Rule","id":"MF_00870","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21565697","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 408 |
| Details | Region: {"description":"Metallo-beta-lactamase N-terminus","evidences":[{"source":"HAMAP-Rule","id":"MF_00870","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21565697","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 386 |
| Details | Region: {"description":"Beta-Casp","evidences":[{"source":"HAMAP-Rule","id":"MF_00870","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21565697","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 116 |
| Details | Region: {"description":"Metallo-beta-lactamase C-terminus","evidences":[{"source":"HAMAP-Rule","id":"MF_00870","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21565697","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00870","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21565697","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2YCB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
