2pid

Crystal structure of human mitochondrial tyrosyl-tRNA synthetase in complex with an adenylate analog

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Tyrosyl-tRNA synthetase

Homo sapiens

UniProt Q9Y2Z4

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 5'-O-[N-(L-TYROSYL)SULFAMOYL]ADENOSINE × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name SYYM_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–348; UniProt 32–375 Author chain B; PDBConstruct 5–348; UniProt 32–375

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id2pid
Deposition date deposition_date2007-04-13
Structure title titleCrystal structure of human mitochondrial tyrosyl-tRNA synthetase in complex with an adenylate analog
Keywords keywordsAMINOACYL-TRNA SYNTHETASE, PROTEIN-SUBSTRATE COMPLEX, ATP-binding, Ligase, Mitochondrion, Nucleotide-binding, Protein biosynthesis; LIGASE
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2pid__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2pid__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

2pid__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)32.73 Å
Rg (electron density)32.91 Å
Total Rg33.24 Å
Atom count5172
Residues641
Excluded volume91920 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2pid__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2pida_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.26 — Adenine nucleotide alpha hydrolase-like
Superfamily Superfamily superfamilyc.26.1 — Nucleotidylyl transferase
Family Family familyc.26.1.0 — automated matches
Domain ID domain_idd2pidb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.26 — Adenine nucleotide alpha hydrolase-like
Superfamily Superfamily superfamilyc.26.1 — Nucleotidylyl transferase
Family Family familyc.26.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id2pidA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily620 — HUPs
Domain ID domain_id2pidA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology240 — Tyrosyl-Transfer RNA Synthetase
Homologous superfamily homologous superfamily10 — Tyrosyl-Transfer RNA Synthetase
Domain ID domain_id2pidB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily620 — HUPs
Domain ID domain_id2pidB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology240 — Tyrosyl-Transfer RNA Synthetase
Homologous superfamily homologous superfamily10 — Tyrosyl-Transfer RNA Synthetase
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7. Citations (2)