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Open data
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Basic information
Entry | Database: PDB / ID: 1qfn | ||||||
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Title | GLUTAREDOXIN-1-RIBONUCLEOTIDE REDUCTASE B1 MIXED DISULFIDE BOND | ||||||
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![]() | ELECTRON TRANSPORT/OXIDOREDUCTASE / GLUTAREDOXIN / RIBONUCLEOTIDE REDUCTASE / DISULFIDE / ELECTRON TRANSFER / ELECTRON TRANSPORT-OXIDOREDUCTASE COMPLEX | ||||||
Function / homology | ![]() cysteine biosynthetic process via S-sulfo-L-cysteine / sulfate assimilation via adenylyl sulfate reduction / protein-disulfide reductase (glutathione) activity / glutathione disulfide oxidoreductase activity / ribonucleoside diphosphate metabolic process / 2'-deoxyribonucleotide biosynthetic process / disulfide oxidoreductase activity / ribonucleoside-diphosphate reductase complex / nucleobase-containing small molecule interconversion / ribonucleoside-diphosphate reductase ...cysteine biosynthetic process via S-sulfo-L-cysteine / sulfate assimilation via adenylyl sulfate reduction / protein-disulfide reductase (glutathione) activity / glutathione disulfide oxidoreductase activity / ribonucleoside diphosphate metabolic process / 2'-deoxyribonucleotide biosynthetic process / disulfide oxidoreductase activity / ribonucleoside-diphosphate reductase complex / nucleobase-containing small molecule interconversion / ribonucleoside-diphosphate reductase / ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor / deoxyribonucleotide biosynthetic process / protein-disulfide reductase activity / protein folding chaperone / cell redox homeostasis / cellular response to oxidative stress / electron transfer activity / nucleotide binding / ATP binding / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / RESTRICTED TORSIONAL ANGLE DYNAMICS | ||||||
![]() | Berardi, M.J. / Bushweller, J.H. | ||||||
![]() | ![]() Title: Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction. Authors: Berardi, M.J. / Bushweller, J.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 651.5 KB | Display | ![]() |
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PDB format | ![]() | 546.4 KB | Display | ![]() |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 9679.759 Da / Num. of mol.: 1 / Mutation: C14S Source method: isolated from a genetically manipulated source Details: INTERMOLECULAR DISULFIDE BRIDGE BETWEEN; CYS 11 A AND CYS 148 B Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 2521.603 Da / Num. of mol.: 1 / Fragment: apha chain, B1 SUBUNIT / Mutation: C754S Source method: isolated from a genetically manipulated source Details: INTERMOLECULAR DISULFIDE BRIDGE CYS759 / Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P00452, ribonucleoside-diphosphate reductase |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Sample conditions | pH: 6.5 / Pressure: 1 atm / Temperature: 293 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
NMR software |
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Refinement | Method: RESTRICTED TORSIONAL ANGLE DYNAMICS / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: LEAST TARGET FUNCTION / Conformers calculated total number: 50 / Conformers submitted total number: 20 |