2cfi

The hydrolase domain of human 10-FTHFD in complex with 6- formyltetrahydropterin

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

10-FORMYLTETRAHYDROFOLATE DEHYDROGENASE

HOMO SAPIENS

UniProt O75891

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 SULFATE ION × 3 6-FORMYLTETRAHYDROPTERIN × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FTHFD_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 23–329; UniProt 1–307

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_id2cfi
Deposition date deposition_date2006-02-21
Structure title titleThe hydrolase domain of human 10-FTHFD in complex with 6- formyltetrahydropterin
Keywords keywordsTETRAHYDROFOLATE, FOLATE BINDING, NADP, ONE-CARBON METABOLISM, OXIDOREDUCTASE, PHOSPHOPANTETHEINE; OXIDOREDUCTASE
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.

2cfi__assembly_1__model_1

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

Download this curve (.dat)

2cfi__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.

2cfi__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)22.55 Å
Rg (electron density)21.84 Å
Total Rg22.74 Å
Atom count2438
Residues310
Excluded volume43460 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2cfi__assembly_1__model_1 monomeric (1) 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 (4)

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6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2cfia1
Class classb — All beta proteins
Fold Fold foldb.46 — FMT C-terminal domain-like
Superfamily Superfamily superfamilyb.46.1 — FMT C-terminal domain-like
Family Family familyb.46.1.1 — Post formyltransferase domain
Domain ID domain_idd2cfia2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.65 — Formyltransferase
Superfamily Superfamily superfamilyc.65.1 — Formyltransferase
Family Family familyc.65.1.1 — Formyltransferase
Domain ID domain_idd2cfia3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id2cfiA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily170 — Formyl transferase, N-terminal domain
Domain ID domain_id2cfiA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology25 — Methionyl-tRNA Fmet Formyltransferase; Chain A, domain 2
Homologous superfamily homologous superfamily10 — Formyl transferase, C-terminal domain
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7. Citations (1)