1YB5
Crystal structure of human Zeta-Crystallin with bound NADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003730 | molecular_function | mRNA 3'-UTR binding |
| A | 0003960 | molecular_function | quinone reductase (NADPH) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0007601 | biological_process | visual perception |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042178 | biological_process | xenobiotic catabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0048255 | biological_process | mRNA stabilization |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070402 | molecular_function | NADPH binding |
| A | 0070404 | molecular_function | NADH binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0003730 | molecular_function | mRNA 3'-UTR binding |
| B | 0003960 | molecular_function | quinone reductase (NADPH) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0007601 | biological_process | visual perception |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042178 | biological_process | xenobiotic catabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0048255 | biological_process | mRNA stabilization |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0070402 | molecular_function | NADPH binding |
| B | 0070404 | molecular_function | NADH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B 811 |
| Chain | Residue |
| A | VAL50 |
| A | TYR53 |
| A | TYR59 |
| A | NAP801 |
| A | HOH986 |
| B | ARG257 |
| B | MET260 |
| B | HOH822 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT A 812 |
| Chain | Residue |
| A | MET260 |
| A | HOH824 |
| B | VAL50 |
| B | TYR53 |
| B | TYR59 |
| B | NAP802 |
| B | HOH950 |
| A | ARG257 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 813 |
| Chain | Residue |
| A | VAL80 |
| A | ASP82 |
| A | HOH1154 |
| B | VAL80 |
| B | GLY81 |
| B | ASP82 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 816 |
| Chain | Residue |
| A | GLY156 |
| A | GLY159 |
| A | GLY160 |
| A | GLY162 |
| A | NAP801 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 817 |
| Chain | Residue |
| B | GLY156 |
| B | GLY159 |
| B | GLY160 |
| B | GLY162 |
| B | NAP802 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A 818 |
| Chain | Residue |
| A | SER97 |
| A | THR98 |
| A | ALA109 |
| A | ALA110 |
| A | THR113 |
| A | HOH870 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 819 |
| Chain | Residue |
| B | GLU51 |
| B | PRO69 |
| B | GLY70 |
| B | HOH864 |
| B | HOH924 |
| B | HOH1155 |
| site_id | AC8 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE NAP A 801 |
| Chain | Residue |
| A | PRO49 |
| A | TYR53 |
| A | ILE131 |
| A | THR135 |
| A | HIS155 |
| A | GLY156 |
| A | SER158 |
| A | GLY159 |
| A | GLY160 |
| A | VAL161 |
| A | ALA180 |
| A | GLY181 |
| A | HIS200 |
| A | LEU225 |
| A | ASN229 |
| A | VAL246 |
| A | ARG249 |
| A | VAL269 |
| A | THR270 |
| A | LEU271 |
| A | ILE315 |
| A | GLY320 |
| A | ALA321 |
| A | CL816 |
| A | HOH833 |
| A | HOH834 |
| A | HOH835 |
| A | HOH906 |
| A | HOH907 |
| A | HOH908 |
| A | HOH909 |
| A | HOH910 |
| A | HOH937 |
| A | HOH938 |
| A | HOH944 |
| A | HOH1073 |
| B | ACT811 |
| B | HOH822 |
| site_id | AC9 |
| Number of Residues | 42 |
| Details | BINDING SITE FOR RESIDUE NAP B 802 |
| Chain | Residue |
| B | VAL246 |
| B | GLY247 |
| B | ARG249 |
| B | VAL269 |
| B | THR270 |
| B | LEU271 |
| B | ILE315 |
| B | GLY320 |
| B | ALA321 |
| B | CL817 |
| B | HOH825 |
| B | HOH867 |
| B | HOH898 |
| B | HOH899 |
| B | HOH900 |
| B | HOH902 |
| B | HOH903 |
| B | HOH905 |
| B | HOH906 |
| B | HOH938 |
| B | HOH944 |
| B | HOH949 |
| B | HOH950 |
| B | HOH1060 |
| B | HOH1063 |
| A | ACT812 |
| A | HOH824 |
| B | PRO49 |
| B | TYR53 |
| B | ILE131 |
| B | THR135 |
| B | HIS155 |
| B | GLY156 |
| B | SER158 |
| B | GLY159 |
| B | GLY160 |
| B | VAL161 |
| B | ALA180 |
| B | GLY181 |
| B | HIS200 |
| B | LEU225 |
| B | ASN229 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 814 |
| Chain | Residue |
| A | ALA171 |
| A | TYR172 |
| A | ILE292 |
| A | TRP294 |
| A | HOH962 |
| A | HOH963 |
| B | ALA171 |
| B | TYR172 |
| B | TRP294 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 815 |
| Chain | Residue |
| A | ASP82 |
| A | ASN83 |
| A | SER85 |
| A | HOH866 |
| A | HOH1152 |
| B | LYS34 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 820 |
| Chain | Residue |
| A | SER301 |
| A | TYR303 |
| A | ASN314 |
| A | SER319 |
| A | GLY320 |
| A | MET325 |
| A | HOH828 |
| A | HOH840 |
| A | HOH1041 |
| A | HOH1131 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 821 |
| Chain | Residue |
| B | SER301 |
| B | TYR303 |
| B | ASN314 |
| B | GLY318 |
| B | SER319 |
| B | GLY320 |
| B | MET325 |
| B | HOH834 |
| B | HOH897 |
| B | HOH1156 |
Functional Information from PROSITE/UniProt
| site_id | PS01162 |
| Number of Residues | 22 |
| Details | QOR_ZETA_CRYSTAL Quinone oxidoreductase / zeta-crystallin signature. GEsvLvhgASGGvGlaacQiaR |
| Chain | Residue | Details |
| A | GLY149-ARG170 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of human zeta-crystallin at 1.85 A.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P47199","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| A | TYR59 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| B | TYR59 |
