9hpq

Peptide-substrate-binding (PSB) domain of human type I collagen prolyl 4-hydroxylase complexed with Pro-Pro-Gly-Pro-Arg-Gly-Pro-Pro-Gly.

Method: X-RAY DIFFRACTION

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

Prolyl 4-hydroxylase subunit alpha-1

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Synthetic peptide PRO-PRO-GLY-PRO-ARG-GLY-PRO-PRO-GLY × 1 MAGNESIUM ION × 1 (4S)-2-METHYL-2,4-PENTANEDIOL × 2 3[N-MORPHOLINO]PROPANE SULFONIC ACID × 1 water × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Synthetic peptide PRO-PRO-GLY-PRO-ARG-GLY-PRO-PRO-GLY × 1 MAGNESIUM ION × 1 (4S)-2-METHYL-2,4-PENTANEDIOL × 1 3[N-MORPHOLINO]PROPANE SULFONIC ACID × 1 GLYCINE × 4 water × 2	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	MAGNESIUM ION × 1 (4S)-2-METHYL-2,4-PENTANEDIOL × 1 3[N-MORPHOLINO]PROPANE SULFONIC ACID × 1 GLYCINE × 1 water × 1	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Synthetic peptide PRO-PRO-GLY-PRO-ARG-GLY-PRO-PRO-GLY × 1 MAGNESIUM ION × 1 (4S)-2-METHYL-2,4-PENTANEDIOL × 2 3[N-MORPHOLINO]PROPANE SULFONIC ACID × 1 GLYCINE × 4 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	P4HA1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–97； UniProt 160–255 Author chain B； PDBConstruct 2–97； UniProt 160–255 Author chain C； PDBConstruct 2–97； UniProt 160–255 Author chain D； PDBConstruct 2–97； UniProt 160–255

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	9hpq
Deposition date deposition_date	2024-12-16
Last revision last_revision	2025-09-24
Structure title title	Peptide-substrate-binding (PSB) domain of human type I collagen prolyl 4-hydroxylase complexed with Pro-Pro-Gly-Pro-Arg-Gly-Pro-Pro-Gly.
Keywords keywords	collagen, tetratricopeptide, extracellular matrix, PROTEIN BINDING; PROTEIN BINDING
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.

9hpq__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

9hpq__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9hpq__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	16.11 Å
Rg (electron density)	15.05 Å
Total Rg	16.07 Å
Atom count	1840
Residues	109
Excluded volume	16558 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9hpq__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`9hpq__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`9hpq__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`9hpq__assembly_4__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 (7)

Entity 1 Entity 1 polymer

Description description	Prolyl 4-hydroxylase subunit alpha-1
Molecular weight formula_weight	12404.9 kDa
EC 编号 ec_number	1.14.11.2
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	7309

MSFLTAEDCFELGKVAYTEADYYHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLKYFEYIMAKELEHHHHHH

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Synthetic peptide PRO-PRO-GLY-PRO-ARG-GLY-PRO-PRO-GLY
Molecular weight formula_weight	831.9 kDa
Source method src_method	syn
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,G

PPGPRGPPG

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 non-polymer

Description description	(4S)-2-METHYL-2,4-PENTANEDIOL
Molecular weight formula_weight	118.2 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 5 Entity 5 non-polymer

Description description	3[N-MORPHOLINO]PROPANE SULFONIC ACID
Molecular weight formula_weight	209.3 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 6 Entity 6 non-polymer

Description description	GLYCINE
Molecular weight formula_weight	75.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	130

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Unit-cell length a length_a	82.418 Å
Unit-cell length b length_b	86.315 Å
Unit-cell length c length_c	91.132 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.170 Å
Low-resolution limit resolution_low	49.880 Å
R factor r_factor	—
R_work r_work	0.2250
R_free r_free	0.2499

Peptide-substrate-binding (PSB) domain of human type I collagen prolyl 4-hydroxylase complexed with Pro-Pro-Gly-Pro-Arg-Gly-Pro-Pro-Gly.

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

Prolyl 4-hydroxylase subunit alpha-1

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

9hpq__assembly_2__model_1

9hpq__assembly_2__model_1 | I(q)

9hpq__assembly_2__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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

7. Citations (1)

Peptide-substrate-binding (PSB) domain of human type I collagen prolyl 4-hydroxylase complexed with Pro-Pro-Gly-Pro-Arg-Gly-Pro-Pro-Gly.

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

Prolyl 4-hydroxylase subunit alpha-1

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

9hpq__assembly_2__model_1

9hpq__assembly_2__model_1 | I(q)

9hpq__assembly_2__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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

7. Citations (1)