2eav

Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ibeta

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

Peptidoglycan recognition protein-I-beta

Homo sapiens

UniProt Q3B822

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 NICKEL (II) ION × 6 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q3B822_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–165; UniProt 209–373 Author chain B; PDBConstruct 1–165; UniProt 209–373

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_id2eav
Deposition date deposition_date2007-02-03
Structure title titleCrystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ibeta
Keywords keywordsALPHA/BETA MIX, SUGAR BINDING PROTEIN; SUGAR BINDING PROTEIN
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.

2eav__assembly_1__model_1

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

Download this curve (.dat)

2eav__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.

2eav__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)22.39 Å
Rg (electron density)21.40 Å
Total Rg22.19 Å
Atom count2524
Residues328
Excluded volume45011 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2eav__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) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2eava_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.118 — N-acetylmuramoyl-L-alanine amidase-like
Superfamily Superfamily superfamilyd.118.1 — N-acetylmuramoyl-L-alanine amidase-like
Family Family familyd.118.1.1 — N-acetylmuramoyl-L-alanine amidase-like
Domain ID domain_idd2eavb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.118 — N-acetylmuramoyl-L-alanine amidase-like
Superfamily Superfamily superfamilyd.118.1 — N-acetylmuramoyl-L-alanine amidase-like
Family Family familyd.118.1.1 — N-acetylmuramoyl-L-alanine amidase-like

CATH v4.4 (2 domains)

Domain ID domain_id2eavA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology80 — Lysozyme-like
Homologous superfamily homologous superfamily10 — Peptidoglycan recognition protein-like
Domain ID domain_id2eavB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology80 — Lysozyme-like
Homologous superfamily homologous superfamily10 — Peptidoglycan recognition protein-like
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7. Citations (1)