1rmq

Crystal structure of AphA class B acid phosphatase/phosphotransferase with osmiate mimicking the catalytic intermediate

Method: X-RAY DIFFRACTION
▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

Class B acid phosphatase

Escherichia coli

UniProt P32697

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 4 COBALT (II) ION × 4 OSMIUM ION × 8 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name APHA_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–212; UniProt 26–237 Author chain B; PDBConstruct 1–212; UniProt 26–237

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1rmq
Deposition date deposition_date2003-11-28
Structure title titleCrystal structure of AphA class B acid phosphatase/phosphotransferase with osmiate mimicking the catalytic intermediate
Keywords keywordsClass B acid phosphatase, DDDD acid phosphatase, metallo-enzyme, osmiate, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
▼

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.

1rmq__assembly_1__model_1

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

Download this curve (.dat)

1rmq__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.

1rmq__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)31.00 Å
Rg (electron density)30.44 Å
Total Rg30.92 Å
Atom count6576
Residues834
Excluded volume116250 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1rmq__assembly_1__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

▼

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1rmqa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.108 — HAD-like
Superfamily Superfamily superfamilyc.108.1 — HAD-like
Family Family familyc.108.1.12 — Class B acid phosphatase, AphA
Domain ID domain_idd1rmqb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.108 — HAD-like
Superfamily Superfamily superfamilyc.108.1 — HAD-like
Family Family familyc.108.1.12 — Class B acid phosphatase, AphA

CATH v4.4 (2 domains)

Domain ID domain_id1rmqA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1000 — HAD superfamily/HAD-like
Domain ID domain_id1rmqB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1000 — HAD superfamily/HAD-like
▶

7. Citations (3)