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 | glucuronate catabolic process to 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 | glucuronate catabolic process to 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: BINDING => ECO:0000269|Ref.11 |
Chain | Residue | Details |
A | VAL16 | |
A | ASP36 | |
A | GLU97 | |
A | LYS102 | |
B | VAL16 | |
B | ASP36 | |
B | GLU97 | |
B | LYS102 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER111 | |
B | SER111 |
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 |