5lhy

PB3 Domain of Human PLK4 (apo)

Method: X-RAY DIFFRACTION

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

Serine/threonine-protein kinase PLK4

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
10	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
11	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
12	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
13	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
14	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
15	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
16	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
17	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
18	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
19	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
20	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
21	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
22	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
23	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
24	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
25	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
26	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
27	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
28	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
29	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
30	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
5	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
6	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
7	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
8	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
9	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PLK4_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 1； PDBConstruct 5–91； UniProt 884–970 Author chain 2； PDBConstruct 5–91； UniProt 884–970 Author chain 3； PDBConstruct 5–91； UniProt 884–970 Author chain 4； PDBConstruct 5–91； UniProt 884–970 Author chain 5； PDBConstruct 5–91； UniProt 884–970 Author chain 6； PDBConstruct 5–91； UniProt 884–970 Author chain 7； PDBConstruct 5–91； UniProt 884–970 Author chain 8； PDBConstruct 5–91； UniProt 884–970 Author chain 9； PDBConstruct 5–91； UniProt 884–970 Author chain A； PDBConstruct 5–91； UniProt 884–970 Author chain B； PDBConstruct 5–91； UniProt 884–970 Author chain C； PDBConstruct 5–91； UniProt 884–970 Author chain D； PDBConstruct 5–91； UniProt 884–970 Author chain E； PDBConstruct 5–91； UniProt 884–970 Author chain F； PDBConstruct 5–91； UniProt 884–970 Author chain G； PDBConstruct 5–91； UniProt 884–970 Author chain H； PDBConstruct 5–91； UniProt 884–970 Author chain I； PDBConstruct 5–91； UniProt 884–970 Author chain J； PDBConstruct 5–91； UniProt 884–970 Author chain K； PDBConstruct 5–91； UniProt 884–970 Author chain L； PDBConstruct 5–91； UniProt 884–970 Author chain M； PDBConstruct 5–91； UniProt 884–970 Author chain N； PDBConstruct 5–91； UniProt 884–970 Author chain O； PDBConstruct 5–91； UniProt 884–970 Author chain P； PDBConstruct 5–91； UniProt 884–970 Author chain Q； PDBConstruct 5–91； UniProt 884–970 Author chain R； PDBConstruct 5–91； UniProt 884–970 Author chain S； PDBConstruct 5–91； UniProt 884–970 Author chain T； PDBConstruct 5–91； UniProt 884–970 Author chain U； PDBConstruct 5–91； UniProt 884–970 Author chain V； PDBConstruct 5–91； UniProt 884–970 Author chain W； PDBConstruct 5–91； UniProt 884–970 Author chain X； PDBConstruct 5–91； UniProt 884–970 Author chain Y； PDBConstruct 5–91； UniProt 884–970 Author chain Z； PDBConstruct 5–91； UniProt 884–970 Author chain a； PDBConstruct 5–91； UniProt 884–970 Author chain b； PDBConstruct 5–91； UniProt 884–970 Author chain c； PDBConstruct 5–91； UniProt 884–970 Author chain d； PDBConstruct 5–91； UniProt 884–970 Author chain e； PDBConstruct 5–91； UniProt 884–970 Author chain f； PDBConstruct 5–91； UniProt 884–970 Author chain g； PDBConstruct 5–91； UniProt 884–970 Author chain h； PDBConstruct 5–91； UniProt 884–970 Author chain i； PDBConstruct 5–91； UniProt 884–970 Author chain j； PDBConstruct 5–91； UniProt 884–970 Author chain k； PDBConstruct 5–91； UniProt 884–970 Author chain l； PDBConstruct 5–91； UniProt 884–970 Author chain m； PDBConstruct 5–91； UniProt 884–970 Author chain n； PDBConstruct 5–91； UniProt 884–970 Author chain o； PDBConstruct 5–91； UniProt 884–970 Author chain p； PDBConstruct 5–91； UniProt 884–970 Author chain q； PDBConstruct 5–91； UniProt 884–970 Author chain r； PDBConstruct 5–91； UniProt 884–970 Author chain s； PDBConstruct 5–91； UniProt 884–970 Author chain t； PDBConstruct 5–91； UniProt 884–970 Author chain u； PDBConstruct 5–91； UniProt 884–970 Author chain v； PDBConstruct 5–91； UniProt 884–970 Author chain w； PDBConstruct 5–91； UniProt 884–970 Author chain x； PDBConstruct 5–91； UniProt 884–970 Author chain y； PDBConstruct 5–91； UniProt 884–970

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	5lhy
Deposition date deposition_date	2016-07-13
Structure title title	PB3 Domain of Human PLK4 (apo)
Keywords keywords	Polo box domain, Centriole, transferase, structural protein; STRUCTURAL 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.

5lhy__assembly_20__model_1

Assembly 20 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5lhy__assembly_20__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5lhy__assembly_20__model_1 | P(r) · Pending

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

Rg（Guinier）	18.64 Å
Rg (electron density)	17.62 Å
Total Rg	18.48 Å
Atom count	1186
Residues	154
Excluded volume	21156 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5lhy__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`5lhy__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`5lhy__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`5lhy__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`5lhy__assembly_5__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`5lhy__assembly_6__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`5lhy__assembly_7__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`5lhy__assembly_8__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
9	1	`5lhy__assembly_9__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
10	1	`5lhy__assembly_10__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
11	1	`5lhy__assembly_11__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
12	1	`5lhy__assembly_12__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
13	1	`5lhy__assembly_13__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
14	1	`5lhy__assembly_14__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
15	1	`5lhy__assembly_15__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
16	1	`5lhy__assembly_16__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
17	1	`5lhy__assembly_17__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
18	1	`5lhy__assembly_18__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
19	1	`5lhy__assembly_19__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
20	1	`5lhy__assembly_20__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
21	1	`5lhy__assembly_21__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
22	1	`5lhy__assembly_22__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
23	1	`5lhy__assembly_23__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
24	1	`5lhy__assembly_24__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
25	1	`5lhy__assembly_25__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
26	1	`5lhy__assembly_26__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
27	1	`5lhy__assembly_27__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
28	1	`5lhy__assembly_28__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
29	1	`5lhy__assembly_29__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
30	1	`5lhy__assembly_30__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 (1)

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6. Fold Classification (SCOP + CATH) 60 domains

CATH v4.4 (60 domains)

Domain ID domain_id	5lhy100
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhy200
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhy300
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhy400
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhy500
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhy600
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhy700
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhy800
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhy900
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyA00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyB00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyC00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyD00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyE00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyF00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyG00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyH00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyI00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyJ00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyK00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyL00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyM00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyN00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyO00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyP00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyQ00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyR00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyS00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyT00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyU00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyV00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyW00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyX00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyY00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyZ00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhya00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyb00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyc00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyd00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhye00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyf00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyg00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyh00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyi00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyj00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyk00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyl00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhym00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyn00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyo00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyp00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyq00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyr00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhys00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyt00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyu00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyv00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyw00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyx00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

Domain ID domain_id	5lhyy00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	930 —

▶

Unit-cell length a length_a	220.350 Å
Unit-cell length b length_b	220.350 Å
Unit-cell length c length_c	325.730 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	480

Space group space_group	P 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	3.310 Å
Low-resolution limit resolution_low	104.367 Å
R factor r_factor	0.2705
R_work r_work	0.2692
R_free r_free	0.2952

Description description	Serine/threonine-protein kinase PLK4
Molecular weight formula_weight	9915.2 kDa
EC 编号 ec_number	2.7.11.21
Source method src_method	man
Copy count entity_count	60

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,Q,R,S,T,U,V,W,X,Y,Z,1,2,3,4,5,6,7,8,9,a,b,c,d,e,f,g,h,i,j,k,l,m,n,o,p,q,r,s,t,u,v,w,x,y
Atom count atom_count	35580

PB3 Domain of Human PLK4 (apo)

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

Serine/threonine-protein kinase PLK4

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

5lhy__assembly_20__model_1

5lhy__assembly_20__model_1 | I(q)

5lhy__assembly_20__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 60 domains

CATH v4.4 (60 domains)

7. Citations (1)

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

PB3 Domain of Human PLK4 (apo)

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

Serine/threonine-protein kinase PLK4

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

5lhy__assembly_20__model_1

5lhy__assembly_20__model_1 | I(q)

5lhy__assembly_20__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 60 domains

CATH v4.4 (60 domains)

7. Citations (1)