1mt5

CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE

Method: X-RAY DIFFRACTION

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

Fatty-acid amide hydrolase

Rattus norvegicus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	METHYL ARACHIDONYL FLUOROPHOSPHONATE × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	METHYL ARACHIDONYL FLUOROPHOSPHONATE × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	METHYL ARACHIDONYL FLUOROPHOSPHONATE × 2	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 2	METHYL ARACHIDONYL FLUOROPHOSPHONATE × 2	Consistent with protein count
5	Protein homooligomer	Homooligomer	Protein 2	METHYL ARACHIDONYL FLUOROPHOSPHONATE × 2	Consistent with protein count
6	Protein homooligomer	Homooligomer	Protein 2	METHYL ARACHIDONYL FLUOROPHOSPHONATE × 2	Consistent with protein count
7	Protein homooligomer	Homooligomer	Protein 2	METHYL ARACHIDONYL FLUOROPHOSPHONATE × 2	Consistent with protein count
8	Protein homooligomer	Homooligomer	Protein 2	METHYL ARACHIDONYL FLUOROPHOSPHONATE × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FAAH_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–537； UniProt 37–573 Author chain B； PDBConstruct 1–537； UniProt 37–573 Author chain C； PDBConstruct 1–537； UniProt 37–573 Author chain D； PDBConstruct 1–537； UniProt 37–573 Author chain E； PDBConstruct 1–537； UniProt 37–573 Author chain F； PDBConstruct 1–537； UniProt 37–573 Author chain G； PDBConstruct 1–537； UniProt 37–573 Author chain H； PDBConstruct 1–537； UniProt 37–573 Author chain I； PDBConstruct 1–537； UniProt 37–573 Author chain J； PDBConstruct 1–537； UniProt 37–573 Author chain K； PDBConstruct 1–537； UniProt 37–573 Author chain L； PDBConstruct 1–537； UniProt 37–573 Author chain M； PDBConstruct 1–537； UniProt 37–573 Author chain N； PDBConstruct 1–537； UniProt 37–573 Author chain O； PDBConstruct 1–537； UniProt 37–573 Author chain P； PDBConstruct 1–537； UniProt 37–573

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	1mt5
Deposition date deposition_date	2002-09-20
Structure title title	CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE
Keywords keywords	AMIDASE SIGNATURE, HYDROLASE; HYDROLASE
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.

1mt5__assembly_7__model_1

Assembly 7 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1mt5__assembly_7__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1mt5__assembly_7__model_1 | P(r) · Pending

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

Rg（Guinier）	31.50 Å
Rg (electron density)	30.58 Å
Total Rg	31.20 Å
Atom count	8066
Residues	1074
Excluded volume	145060 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1mt5__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1mt5__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1mt5__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1mt5__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`1mt5__assembly_5__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`1mt5__assembly_6__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`1mt5__assembly_7__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`1mt5__assembly_8__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 (2)

Entity 1 Entity 1 polymer

Description description	Fatty-acid amide hydrolase
Molecular weight formula_weight	58943.0 kDa
EC 编号 ec_number	3.1.-.-
Source method src_method	man
Copy count entity_count	16

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P
Atom count atom_count	64524

ARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLPLLQLVQKLQSGELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHDSTLGLSLNEGMPSESDCVVVQVLKLQGAVPFVHTNVPQSMLSFDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQTAVQLSLGPMARDVESLALCLKALLCEHLFTLDPTVPPLPFREEVYRSSRPLRVGYYETDNYTMPSPAMRRALIETKQRLEAAGHTLIPFLPNNIPYALEVLSAGGLFSDGGRSFLQNFKGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAAFLNSMRPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLTPMLGPALDLNTPGRATGAISYTVLYNCLDFPAGVVPVTTVTAEDDAQMELYKGYFGDIWDIILKKAMKNSVGLPVAVQCVALPWQEELCLRFMREVEQLMT

Source Source

Source organism organism	Rattus norvegicus
Common name common_name	Norway rat
NCBI taxonomy ID ncbi_taxonomy_id	10116
Host organism host_organism	Escherichia coli BL21

Entity 2 Entity 2 non-polymer

Description description	METHYL ARACHIDONYL FLUOROPHOSPHONATE
Molecular weight formula_weight	370.5 kDa
Source method src_method	syn
Copy count entity_count	16

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6. Fold Classification (SCOP + CATH) 32 domains

SCOP 2.08 (16 domains)

Domain ID domain_id	d1mt5a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5d_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5e_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5f_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5g_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5h_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5i_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5j_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5k_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5l_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5m_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5n_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5o_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

Domain ID domain_id	d1mt5p_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.117 — Amidase signature (AS) enzymes
Superfamily Superfamily superfamily	c.117.1 — Amidase signature (AS) enzymes
Family Family family	c.117.1.1 — Amidase signature (AS) enzymes

CATH v4.4 (16 domains)

Domain ID domain_id	1mt5A00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5B00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5C00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5D00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5E00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5F00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5G00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5H00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5I00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5J00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5K00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5L00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5M00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5N00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5O00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

Domain ID domain_id	1mt5P00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1300 — Amidase signature (AS) enzymes
Homologous superfamily homologous superfamily	10 — Amidase signature (AS) domain

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Unit-cell length a length_a	147.107 Å
Unit-cell length b length_b	272.019 Å
Unit-cell length c length_c	147.216 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	115.21 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	32

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

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	141.420 Å
R factor r_factor	0.2206
R_work r_work	0.2184
R_free r_free	0.2623

CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE

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

Fatty-acid amide hydrolase

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

1mt5__assembly_7__model_1

1mt5__assembly_7__model_1 | I(q)

1mt5__assembly_7__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 non-polymer

6. Fold Classification (SCOP + CATH) 32 domains

SCOP 2.08 (16 domains)

CATH v4.4 (16 domains)

7. Citations (1)

CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE

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

Fatty-acid amide hydrolase

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

1mt5__assembly_7__model_1

1mt5__assembly_7__model_1 | I(q)

1mt5__assembly_7__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 non-polymer

6. Fold Classification (SCOP + CATH) 32 domains

SCOP 2.08 (16 domains)

CATH v4.4 (16 domains)

7. Citations (1)