3F3S
The Crystal Structure of Human Lambda-Crystallin, CRYL1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0019640 | biological_process | D-glucuronate catabolic process to D-xylulose 5-phosphate |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0050104 | molecular_function | L-gulonate 3-dehydrogenase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0019640 | biological_process | D-glucuronate catabolic process to D-xylulose 5-phosphate |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0050104 | molecular_function | L-gulonate 3-dehydrogenase activity |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD A 601 |
| Chain | Residue |
| A | GLY13 |
| A | GLU97 |
| A | LYS102 |
| A | ILE105 |
| A | ASP115 |
| A | SER122 |
| A | THR123 |
| A | SER124 |
| A | PRO146 |
| A | ASN148 |
| A | SO4317 |
| A | GLY15 |
| A | HOH329 |
| A | HOH386 |
| A | HOH429 |
| A | HOH454 |
| A | HOH485 |
| A | HOH546 |
| A | HOH547 |
| A | HOH559 |
| A | VAL16 |
| A | ILE17 |
| A | ASP36 |
| A | ILE37 |
| A | CYS94 |
| A | VAL95 |
| A | PRO96 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1 |
| Chain | Residue |
| A | TRP207 |
| A | GLU211 |
| A | PRO270 |
| A | GLU271 |
| A | PHE272 |
| A | SER273 |
| A | THR276 |
| A | HOH363 |
| A | HOH461 |
| A | HOH618 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 317 |
| Chain | Residue |
| A | SER124 |
| A | HOH342 |
| A | HOH430 |
| A | HOH488 |
| A | HOH585 |
| A | HOH590 |
| A | NAD601 |
| B | TYR255 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 318 |
| Chain | Residue |
| A | ARG274 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 2 |
| Chain | Residue |
| A | GLN39 |
| A | ARG43 |
| A | HOH378 |
| A | HOH420 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 3 |
| Chain | Residue |
| A | HIS261 |
| A | GLN264 |
| A | HOH351 |
| B | LEU46 |
| B | ARG50 |
| B | GLY77 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD B 601 |
| Chain | Residue |
| A | ASN244 |
| A | TYR255 |
| A | HOH419 |
| B | GLY13 |
| B | GLY15 |
| B | VAL16 |
| B | ILE17 |
| B | ASP36 |
| B | ILE37 |
| B | CYS94 |
| B | VAL95 |
| B | PRO96 |
| B | GLU97 |
| B | LYS102 |
| B | SER122 |
| B | SER124 |
| B | HIS145 |
| B | PRO146 |
| B | ASN148 |
| B | SO4317 |
| B | GOL320 |
| B | HOH340 |
| B | HOH439 |
| B | HOH452 |
| B | HOH490 |
| B | HOH548 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2 |
| Chain | Residue |
| B | TRP207 |
| B | GLU211 |
| B | PRO270 |
| B | GLU271 |
| B | PHE272 |
| B | SER273 |
| B | THR276 |
| B | HOH438 |
| B | HOH552 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 317 |
| Chain | Residue |
| B | NAD601 |
| A | ARG231 |
| B | HIS145 |
| B | VAL147 |
| B | ASN148 |
| B | LEU195 |
| B | ASN196 |
| B | GLN199 |
| B | GOL320 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 1 |
| Chain | Residue |
| B | GLY64 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 318 |
| Chain | Residue |
| B | HIS173 |
| B | LYS177 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 3 |
| Chain | Residue |
| B | MET127 |
| B | LYS130 |
| B | HOH576 |
| B | HOH612 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 319 |
| Chain | Residue |
| A | ARG197 |
| B | GLU205 |
| B | ARG208 |
| B | PHE266 |
| B | GLY267 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 320 |
| Chain | Residue |
| A | ASN244 |
| A | TYR251 |
| A | TYR255 |
| B | SER124 |
| B | ASN196 |
| B | TYR200 |
| B | SO4317 |
| B | HOH425 |
| B | NAD601 |
Functional Information from PROSITE/UniProt
| site_id | PS00067 |
| Number of Residues | 25 |
| Details | 3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. EvaGFVlNRlqyAIIseawr.LVeeG |
| Chain | Residue | Details |
| A | GLU189-GLY213 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of human lambda-crystallin, CRYL1.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 2hdh |
| Chain | Residue | Details |
| A | HIS145 | |
| A | SER124 | |
| A | ASN196 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 2hdh |
| Chain | Residue | Details |
| B | HIS145 | |
| B | SER124 | |
| B | ASN196 |
