3G4H
Crystal structure of Human Senescence Marker Protein-30 (Zinc Bound)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004341 | molecular_function | gluconolactonase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0006874 | biological_process | intracellular calcium ion homeostasis |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0030234 | molecular_function | enzyme regulator activity |
A | 0032781 | biological_process | positive regulation of ATP-dependent activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0050848 | biological_process | regulation of calcium-mediated signaling |
B | 0004341 | molecular_function | gluconolactonase activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0006874 | biological_process | intracellular calcium ion homeostasis |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0030234 | molecular_function | enzyme regulator activity |
B | 0032781 | biological_process | positive regulation of ATP-dependent activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0050848 | biological_process | regulation of calcium-mediated signaling |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 300 |
Chain | Residue |
A | GLU18 |
A | ASN154 |
A | ASP204 |
A | HOH315 |
A | HOH326 |
A | HOH356 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 300 |
Chain | Residue |
B | HOH344 |
B | GLU18 |
B | ASN154 |
B | ASP204 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:23349732 |
Chain | Residue | Details |
B | ASP204 | |
A | ASP204 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23349732 |
Chain | Residue | Details |
B | GLU18 | |
B | ASN154 | |
B | ASP204 | |
A | GLU18 | |
A | ASN154 | |
A | ASP204 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
B | ARG101 | |
B | ASN103 | |
A | ARG101 | |
A | ASN103 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
B | GLU121 | |
A | GLU121 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q64374 |
Chain | Residue | Details |
B | LYS144 | |
B | LYS244 | |
B | LYS253 | |
A | LYS144 | |
A | LYS244 | |
A | LYS253 |