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1erz

CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES

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

N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE

Agrobacterium sp.

UniProt P60327

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 4 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

Monomer

None

Homodimer
8hpc 8hpc 8hpc 8hpc

4 assemblies

Homotetramer
1erz 1uf4 1uf5 1uf7 1uf8

5 assemblies

Other homooligomers

None

Heteromeric or nucleic-acid complex

None

View Construct and Data Evidence
UniProt name DCAS_AGRSK
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–303； UniProt 2–304 Author chain B； PDBConstruct 1–303； UniProt 2–304

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_id1erz
Deposition date deposition_date2000-04-06
Structure title titleCRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES
Keywords keywordsfour-layer sandwich, HYDROLASE; HYDROLASE
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.

1erz__assembly_1__model_1

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

Download this curve (.dat)

1erz__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1erz__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）30.99 Å
Rg (electron density)30.17 Å
Total Rg30.89 Å
Atom count9628
Residues1212
Excluded volume170940 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1erz__assembly_1__model_1 tetrameric （4） 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 (2)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1erza_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.160 — Carbon-nitrogen hydrolase
Superfamily Superfamily superfamilyd.160.1 — Carbon-nitrogen hydrolase
Family Family familyd.160.1.2 — Carbamilase
Domain ID domain_idd1erzb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.160 — Carbon-nitrogen hydrolase
Superfamily Superfamily superfamilyd.160.1 — Carbon-nitrogen hydrolase
Family Family familyd.160.1.2 — Carbamilase

CATH v4.4 (2 domains)

Domain ID domain_id1erzA00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology110 — Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase
Homologous superfamily homologous superfamily10 — Carbon-nitrogen hydrolase
Domain ID domain_id1erzB00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology110 — Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase
Homologous superfamily homologous superfamily10 — Carbon-nitrogen hydrolase
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7. Citations (3)