SAXSdb — 1cb7

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

PROTEIN (GLUTAMATE MUTASE)

Clostridium cochlearium

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	PROTEIN (GLUTAMATE MUTASE) × 2 （P80077） CO-METHYLCOBALAMIN × 2 D(-)-TARTARIC ACID × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MAMA_CLOCO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–137； UniProt 1–137 Author chain C； PDBConstruct 1–137； UniProt 1–137

PROTEIN (GLUTAMATE MUTASE)

Clostridium cochlearium

UniProt P80077

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	PROTEIN (GLUTAMATE MUTASE) × 2 （P80078） CO-METHYLCOBALAMIN × 2 D(-)-TARTARIC ACID × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	GLME_CLOCO
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–483； UniProt 1–483 Author chain D； PDBConstruct 1–483； UniProt 1–483

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	1cb7
Deposition date deposition_date	1999-03-03
Structure title title	GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM RECONSTITUTED WITH METHYL-COBALAMIN
Keywords keywords	GLUTAMATE MUTASE, COENZYME-B12, RADICAL REACTION, TIM-BARREL, ROSSMAN-FOLD, ISOMERASE; ISOMERASE
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.

1cb7__assembly_1__model_1

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

Download this curve (.dat)

1cb7__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1cb7__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	33.96 Å
Rg (electron density)	33.37 Å
Total Rg	33.88 Å
Atom count	9810
Residues	1240
Excluded volume	175410 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1cb7__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 (5)

Entity 1 Entity 1 polymer

Description description	PROTEIN (GLUTAMATE MUTASE)
Molecular weight formula_weight	14830.0 kDa
EC 编号 ec_number	5.4.99.1
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	10825

MEKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDEAGLEGILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKKDLNIE

Source Source

Source organism organism	Clostridium cochlearium
NCBI taxonomy ID ncbi_taxonomy_id	1494
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	PROTEIN (GLUTAMATE MUTASE)
Molecular weight formula_weight	53623.2 kDa
EC 编号 ec_number	5.4.99.1
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

MELKNKKWTDEEFHKQREEVLQQWPTGKEVDLQEAVDYLKKIPAEKNFAEKLVLAKKKGITMAQPRAGVALLDEHIELLRYLQDEGGADFLPSTIDAYTRQNRYDECENGIKESEKAGRSLLNGFPGVNFGVKGCRKVLEAVNLPLQARHGTPDSRLLAEIIHAGGWTSNEGGGISYNVPYAKNVTIEKSLLDWQYCDRLVGFYEEQGVHINREPFGPLTGTLVPPSMSNAVGITEALLAAEQGVKNITVGYGECGNMIQDIAALRCLEEQTNEYLKAYGYNDVFVTTVFHQWMGGFPQDESKAFGVIVTATTIAALAGATKVIVKTPHEAIGIPTKEANAAGIKATKMALNMLEGQRMPMSKELETEMAVIKAETKCILDKMFELGKGDLAIGTVKAFETGVMDIPFGPSKYNAGKMMPVRDNLGCVRYLEFGNVPFTEEIKNYNRERLQERAKFEGRDVSFQMVIDDIFAVGKGRLIGRPE

Source Source

Source organism organism	Clostridium cochlearium
NCBI taxonomy ID ncbi_taxonomy_id	1494
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	CO-METHYLCOBALAMIN
Molecular weight formula_weight	1344.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	D(-)-TARTARIC ACID
Molecular weight formula_weight	150.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1013

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1cb7a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.23 — Flavodoxin-like
Superfamily Superfamily superfamily	c.23.6 — Cobalamin (vitamin B12)-binding domain
Family Family family	c.23.6.1 — Cobalamin (vitamin B12)-binding domain

Domain ID domain_id	d1cb7b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.19 — Cobalamin (vitamin B12)-dependent enzymes
Family Family family	c.1.19.2 — Glutamate mutase, large subunit

Domain ID domain_id	d1cb7c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.23 — Flavodoxin-like
Superfamily Superfamily superfamily	c.23.6 — Cobalamin (vitamin B12)-binding domain
Family Family family	c.23.6.1 — Cobalamin (vitamin B12)-binding domain

Domain ID domain_id	d1cb7d_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.19 — Cobalamin (vitamin B12)-dependent enzymes
Family Family family	c.1.19.2 — Glutamate mutase, large subunit

CATH v4.4 (6 domains)

Domain ID domain_id	1cb7A00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	280 — Cobalamin-binding domain

Domain ID domain_id	1cb7B01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	240 — Methylmalonyl-CoA mutase

Domain ID domain_id	1cb7B02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	970 — Glutamate mutase, C-terminal domain
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1cb7C00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	280 — Cobalamin-binding domain

Domain ID domain_id	1cb7D01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	240 — Methylmalonyl-CoA mutase

Domain ID domain_id	1cb7D02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	970 — Glutamate mutase, C-terminal domain
Homologous superfamily homologous superfamily	10 —

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Unit-cell length a length_a	64.330 Å
Unit-cell length b length_b	113.140 Å
Unit-cell length c length_c	108.610 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	95.62 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	25.000 Å
R factor r_factor	0.1597
R_work r_work	—
R_free r_free	0.2185

GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM RECONSTITUTED WITH METHYL-COBALAMIN

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

PROTEIN (GLUTAMATE MUTASE)

State in the Current Structure

Other States of the Same Protein in the Database

PROTEIN (GLUTAMATE MUTASE)

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

1cb7__assembly_1__model_1

1cb7__assembly_1__model_1 | I(q)

1cb7__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

CATH v4.4 (6 domains)

7. Citations (3)

GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM RECONSTITUTED WITH METHYL-COBALAMIN

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

PROTEIN (GLUTAMATE MUTASE)

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

PROTEIN (GLUTAMATE MUTASE)

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

1cb7__assembly_1__model_1

1cb7__assembly_1__model_1 | I(q)

1cb7__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

CATH v4.4 (6 domains)

7. Citations (3)