3mm0

Crystal structure of chimeric avidin

Method: X-RAY DIFFRACTION

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

Avidin, Avidin-related protein 4/5

Gallus gallus

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	AVID_CHICK
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–40； UniProt 25–61 Author chain A； PDBConstruct 62–129； UniProt 85–152 Author chain B； PDBConstruct 4–40； UniProt 25–61 Author chain B； PDBConstruct 62–129； UniProt 85–152 Author chain C； PDBConstruct 4–40； UniProt 25–61 Author chain C； PDBConstruct 62–129； UniProt 85–152 Author chain D； PDBConstruct 4–40； UniProt 25–61 Author chain D； PDBConstruct 62–129； UniProt 85–152 Author chain E； PDBConstruct 4–40； UniProt 25–61 Author chain E； PDBConstruct 62–129； UniProt 85–152 Author chain F； PDBConstruct 4–40； UniProt 25–61 Author chain F； PDBConstruct 62–129； UniProt 85–152 Author chain G； PDBConstruct 4–40； UniProt 25–61 Author chain G； PDBConstruct 62–129； UniProt 85–152 Author chain H； PDBConstruct 4–40； UniProt 25–61 Author chain H； PDBConstruct 62–129； UniProt 85–152 Author chain I； PDBConstruct 4–40； UniProt 25–61 Author chain I； PDBConstruct 62–129； UniProt 85–152 Author chain K； PDBConstruct 4–40； UniProt 25–61 Author chain K； PDBConstruct 62–129； UniProt 85–152 Author chain M； PDBConstruct 4–40； UniProt 25–61 Author chain M； PDBConstruct 62–129； UniProt 85–152 Author chain N； PDBConstruct 4–40； UniProt 25–61 Author chain N； PDBConstruct 62–129； UniProt 85–152

Avidin, Avidin-related protein 4/5

Gallus gallus

UniProt P56734

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	AVR4_CHICK
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 41–61； UniProt 62–82 Author chain B； PDBConstruct 41–61； UniProt 62–82 Author chain C； PDBConstruct 41–61； UniProt 62–82 Author chain D； PDBConstruct 41–61； UniProt 62–82 Author chain E； PDBConstruct 41–61； UniProt 62–82 Author chain F； PDBConstruct 41–61； UniProt 62–82 Author chain G； PDBConstruct 41–61； UniProt 62–82 Author chain H； PDBConstruct 41–61； UniProt 62–82 Author chain I； PDBConstruct 41–61； UniProt 62–82 Author chain K； PDBConstruct 41–61； UniProt 62–82 Author chain M； PDBConstruct 41–61； UniProt 62–82 Author chain N； PDBConstruct 41–61； UniProt 62–82

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_id	3mm0
Deposition date deposition_date	2010-04-19
Structure title title	Crystal structure of chimeric avidin
Keywords keywords	avidin, AVR4, high affinity systems, hyper-thermostability, BIOTIN BINDING PROTEIN; BIOTIN BINDING PROTEIN
Experimental Method method	X-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.

3mm0__assembly_1__model_1

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

Download this curve (.dat)

3mm0__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3mm0__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	22.45 Å
Rg (electron density)	21.35 Å
Total Rg	22.38 Å
Atom count	3632
Residues	467
Excluded volume	64556 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3mm0__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3mm0__assembly_2__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3mm0__assembly_3__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`3mm0__assembly_4__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) 24 domains

SCOP 2.08 (12 domains)

Domain ID domain_id	d3mm0a_
Class class	b — All beta proteins
Fold Fold fold	b.61 — Streptavidin-like
Superfamily Superfamily superfamily	b.61.1 — Avidin/streptavidin
Family Family family	b.61.1.1 — Avidin/streptavidin

Domain ID domain_id	d3mm0b_
Class class	b — All beta proteins
Fold Fold fold	b.61 — Streptavidin-like
Superfamily Superfamily superfamily	b.61.1 — Avidin/streptavidin
Family Family family	b.61.1.1 — Avidin/streptavidin

Domain ID domain_id	d3mm0c_
Class class	b — All beta proteins
Fold Fold fold	b.61 — Streptavidin-like
Superfamily Superfamily superfamily	b.61.1 — Avidin/streptavidin
Family Family family	b.61.1.1 — Avidin/streptavidin

Domain ID domain_id	d3mm0d_
Class class	b — All beta proteins
Fold Fold fold	b.61 — Streptavidin-like
Superfamily Superfamily superfamily	b.61.1 — Avidin/streptavidin
Family Family family	b.61.1.1 — Avidin/streptavidin

Domain ID domain_id	d3mm0e_
Class class	b — All beta proteins
Fold Fold fold	b.61 — Streptavidin-like
Superfamily Superfamily superfamily	b.61.1 — Avidin/streptavidin
Family Family family	b.61.1.1 — Avidin/streptavidin

Domain ID domain_id	d3mm0f_
Class class	b — All beta proteins
Fold Fold fold	b.61 — Streptavidin-like
Superfamily Superfamily superfamily	b.61.1 — Avidin/streptavidin
Family Family family	b.61.1.1 — Avidin/streptavidin

Domain ID domain_id	d3mm0g_
Class class	b — All beta proteins
Fold Fold fold	b.61 — Streptavidin-like
Superfamily Superfamily superfamily	b.61.1 — Avidin/streptavidin
Family Family family	b.61.1.1 — Avidin/streptavidin

Domain ID domain_id	d3mm0h_
Class class	b — All beta proteins
Fold Fold fold	b.61 — Streptavidin-like
Superfamily Superfamily superfamily	b.61.1 — Avidin/streptavidin
Family Family family	b.61.1.1 — Avidin/streptavidin

Domain ID domain_id	d3mm0i_
Class class	b — All beta proteins
Fold Fold fold	b.61 — Streptavidin-like
Superfamily Superfamily superfamily	b.61.1 — Avidin/streptavidin
Family Family family	b.61.1.1 — Avidin/streptavidin

Domain ID domain_id	d3mm0k_
Class class	b — All beta proteins
Fold Fold fold	b.61 — Streptavidin-like
Superfamily Superfamily superfamily	b.61.1 — Avidin/streptavidin
Family Family family	b.61.1.1 — Avidin/streptavidin

Domain ID domain_id	d3mm0m_
Class class	b — All beta proteins
Fold Fold fold	b.61 — Streptavidin-like
Superfamily Superfamily superfamily	b.61.1 — Avidin/streptavidin
Family Family family	b.61.1.1 — Avidin/streptavidin

Domain ID domain_id	d3mm0n_
Class class	b — All beta proteins
Fold Fold fold	b.61 — Streptavidin-like
Superfamily Superfamily superfamily	b.61.1 — Avidin/streptavidin
Family Family family	b.61.1.1 — Avidin/streptavidin

CATH v4.4 (12 domains)

Domain ID domain_id	3mm0A00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	30 — Avidin-like

Domain ID domain_id	3mm0B00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	30 — Avidin-like

Domain ID domain_id	3mm0C00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	30 — Avidin-like

Domain ID domain_id	3mm0D00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	30 — Avidin-like

Domain ID domain_id	3mm0E00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	30 — Avidin-like

Domain ID domain_id	3mm0F00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	30 — Avidin-like

Domain ID domain_id	3mm0G00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	30 — Avidin-like

Domain ID domain_id	3mm0H00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	30 — Avidin-like

Domain ID domain_id	3mm0I00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	30 — Avidin-like

Domain ID domain_id	3mm0K00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	30 — Avidin-like

Domain ID domain_id	3mm0M00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	30 — Avidin-like

Domain ID domain_id	3mm0N00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	30 — Avidin-like

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Unit-cell length a length_a	158.657 Å
Unit-cell length b length_b	124.791 Å
Unit-cell length c length_c	88.895 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	114.45 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	48

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.2259
R_work r_work	0.2218
R_free r_free	0.3093

Description description	Avidin, Avidin-related protein 4/5
Molecular weight formula_weight	14400.3 kDa
Mutation mutation	I141Y
Source method src_method	man
Copy count entity_count	12

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,K,M,N
Atom count atom_count	11014

Crystal structure of chimeric avidin

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

Avidin, Avidin-related protein 4/5

State in the Current Structure

Other States of the Same Protein in the Database

Avidin, Avidin-related protein 4/5

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3mm0__assembly_1__model_1

3mm0__assembly_1__model_1 | I(q)

3mm0__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

CATH v4.4 (12 domains)

7. Citations (1)

Source organism organism	Gallus gallus
Common name common_name	bantam,chickens
NCBI taxonomy ID ncbi_taxonomy_id	9031
Host organism host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	91

Crystal structure of chimeric avidin

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

Avidin, Avidin-related protein 4/5

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Avidin, Avidin-related protein 4/5

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3mm0__assembly_1__model_1

3mm0__assembly_1__model_1 | I(q)

3mm0__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

CATH v4.4 (12 domains)

7. Citations (1)