Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4LLB

Crystal Structure of MOZ double PHD finger histone H3K14ac complex

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0000786	cellular_component	nucleosome
C	0003677	molecular_function	DNA binding
C	0030527	molecular_function	structural constituent of chromatin
D	0000786	cellular_component	nucleosome
D	0003677	molecular_function	DNA binding
D	0030527	molecular_function	structural constituent of chromatin

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	CYS281
A	CYS284
A	CYS307
A	CYS310

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 402

Chain	Residue
A	CYS265
A	CYS268
A	HIS289
A	CYS292

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 403

Chain	Residue
A	CYS212
A	HIS238
A	CYS241
A	CYS209

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 404

Chain	Residue
A	CYS230
A	CYS233
A	CYS259
A	CYS262

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 401

Chain	Residue
B	CYS281
B	CYS284
B	CYS307
B	CYS310

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 402

Chain	Residue
B	CYS265
B	CYS268
B	HIS289
B	CYS292

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 403

Chain	Residue
B	CYS209
B	CYS212
B	HIS238
B	CYS241

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 404

Chain	Residue
B	CYS230
B	CYS233
B	CYS259
B	CYS262

site_id	AC9
Number of Residues	56
Details	BINDING SITE FOR CHAIN B OF HISTONE ACETYLTRANSFERASE KAT6A

Chain	Residue
A	GLU221
A	VAL250
B	LEU192
B	LEU192
B	GLU193
B	ZN401
B	ZN402
B	ZN403
B	ZN404
B	HOH501
B	HOH502
B	HOH503
B	HOH504
B	HOH505
B	HOH506
B	HOH508
B	HOH509
B	HOH510
B	HOH511
B	HOH511
B	HOH512
B	HOH513
B	HOH515
B	HOH518
B	HOH519
B	HOH520
B	HOH522
B	HOH523
B	HOH524
B	HOH525
B	HOH526
B	HOH528
B	HOH530
B	HOH532
B	HOH533
B	HOH535
B	HOH538
B	HOH539
B	HOH540
B	HOH541
B	HOH542
B	HOH543
B	HOH558
D	ALA1
D	ARG2
D	THR3
D	LYS4
D	GLN5
D	ALA7
D	ARG8
D	SER10
D	THR11
D	GLY13
D	ALY14
D	ALA15
D	HOH103

Functional Information from PROSITE/UniProt

site_id	PS00322
Number of Residues	7
Details	HISTONE_H3_1 Histone H3 signature 1. KAPRKQL

Chain	Residue	Details
C	ALY14-LEU20

site_id	PS01359
Number of Residues	81
Details	ZF_PHD_1 Zinc finger PHD-type signature. CadCgnsghpsclkfspeltvrvkalrwqciecktcsscrdqgknadnmLfCds..Cdrg.FHmeCcdppltrmpkgm.................................WiCqiC

Chain	Residue	Details
A	CYS230-CYS310

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Citrulline; alternate => ECO:0000269\|PubMed:16567635

Chain	Residue	Details
C	ARG2
D	ARG2

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by HASPIN and VRK1 => ECO:0000269\|PubMed:15681610, ECO:0000269\|PubMed:16185088, ECO:0000269\|PubMed:31527692

Chain	Residue	Details
C	THR3
D	THR3

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:16267050, ECO:0000269\|PubMed:16457588, ECO:0000269\|PubMed:17194708

Chain	Residue	Details
C	LYS4
D	LYS4

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269\|PubMed:30867594

Chain	Residue	Details
C	GLN5
D	GLN5

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PKC => ECO:0000269\|PubMed:20228790

Chain	Residue	Details
C	THR6
D	THR6

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250\|UniProtKB:P68433

Chain	Residue	Details
C	ARG8
D	ARG8

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:11242053, ECO:0000269\|PubMed:16185088, ECO:0000269\|PubMed:16267050, ECO:0000269\|PubMed:16457588, ECO:0000269\|PubMed:17194708

Chain	Residue	Details
C	LYS9
D	LYS9

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269\|PubMed:10464286, ECO:0000269\|PubMed:11856369, ECO:0000269\|PubMed:12560483, ECO:0000269\|PubMed:15681610, ECO:0000269\|PubMed:16185088, ECO:0000269\|PubMed:16457588

Chain	Residue	Details
C	SER10
D	SER10

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PKC and CHEK1 => ECO:0000269\|PubMed:12560483, ECO:0000269\|PubMed:18066052, ECO:0000269\|PubMed:18243098, ECO:0000269\|PubMed:22901803

Chain	Residue	Details
C	THR11
D	THR11

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:22389435

Chain	Residue	Details
C	ALY14
D	ALY14

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Citrulline; alternate => ECO:0000269\|PubMed:15345777, ECO:0000269\|PubMed:16497732, ECO:0000269\|PubMed:16567635

Chain	Residue	Details
C	ARG17
D	ARG17

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:16267050, ECO:0000269\|PubMed:17194708

Chain	Residue	Details
C	LYS18
D	LYS18

site_id	SWS_FT_FI13
Number of Residues	2
Details	LIPID: N6-decanoyllysine => ECO:0000269\|PubMed:35939806

Chain	Residue	Details
C	LYS18
D	LYS18

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)