Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6F56

Mutant of Human N-myristoyltransferase with bound myristoyl-CoA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004379	molecular_function	glycylpeptide N-tetradecanoyltransferase activity
A	0006499	biological_process	N-terminal protein myristoylation
B	0004379	molecular_function	glycylpeptide N-tetradecanoyltransferase activity
B	0006499	biological_process	N-terminal protein myristoylation
C	0004379	molecular_function	glycylpeptide N-tetradecanoyltransferase activity
C	0006499	biological_process	N-terminal protein myristoylation
D	0004379	molecular_function	glycylpeptide N-tetradecanoyltransferase activity
D	0006499	biological_process	N-terminal protein myristoylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	binding site for residue MYA A 501

Chain	Residue
A	TYR117
A	CYS249
A	VAL250
A	ARG255
A	SER256
A	LYS257
A	ARG258
A	VAL259
A	ALA260
A	PRO261
A	THR268
A	GLN118
A	PHE277
A	TYR281
A	THR282
A	LEU287
A	TYR479
A	MG502
A	HOH654
A	PHE119
A	TRP120
A	ASN179
A	TYR180
A	VAL181
A	PHE247
A	LEU248

site_id	AC2
Number of Residues	7
Details	binding site for residue MG A 502

Chain	Residue
A	LEU254
A	ARG255
A	SER256
A	LYS257
A	ARG258
A	VAL259
A	MYA501

site_id	AC3
Number of Residues	7
Details	binding site for residue GOL A 503

Chain	Residue
A	PRO126
A	LYS289
A	VAL291
A	LEU478
A	TRP481
A	LYS482
A	CYS483

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 504

Chain	Residue
A	GLU244
A	TRP374
A	TYR423
A	VAL494
A	HOH699

site_id	AC5
Number of Residues	31
Details	binding site for residue MYA B 501

Chain	Residue
B	TYR117
B	GLN118
B	PHE119
B	TRP120
B	ASN179
B	TYR180
B	VAL181
B	ASN246
B	PHE247
B	LEU248
B	CYS249
B	VAL250
B	ARG255
B	SER256
B	LYS257
B	ARG258
B	VAL259
B	ALA260
B	PRO261
B	THR268
B	PHE277
B	ALA279
B	TYR281
B	THR282
B	ALA283
B	LEU287
B	ASN317
B	TYR479
B	MG502
B	HOH684
B	HOH695

site_id	AC6
Number of Residues	6
Details	binding site for residue MG B 502

Chain	Residue
B	LEU254
B	SER256
B	LYS257
B	ARG258
B	VAL259
B	MYA501

site_id	AC7
Number of Residues	7
Details	binding site for residue GOL B 503

Chain	Residue
B	PRO126
B	LYS289
B	VAL291
B	LEU478
B	TRP481
B	LYS482
B	CYS483

site_id	AC8
Number of Residues	7
Details	binding site for residue GOL B 504

Chain	Residue
B	GLU244
B	PRO364
B	TRP374
B	PHE422
B	TYR423
B	VAL494
B	HOH610

site_id	AC9
Number of Residues	27
Details	binding site for residue MYA C 501

Chain	Residue
C	TRP120
C	ASN179
C	TYR180
C	VAL181
C	PHE247
C	LEU248
C	CYS249
C	VAL250
C	ARG255
C	SER256
C	ARG258
C	VAL259
C	ALA260
C	PRO261
C	THR268
C	VAL271
C	PHE277
C	GLN278
C	TYR281
C	THR282
C	LEU287
C	TYR479
C	MG502
C	HOH615
C	TYR117
C	GLN118
C	PHE119

site_id	AD1
Number of Residues	7
Details	binding site for residue MG C 502

Chain	Residue
C	LEU254
C	ARG255
C	SER256
C	LYS257
C	ARG258
C	VAL259
C	MYA501

site_id	AD2
Number of Residues	7
Details	binding site for residue GOL C 503

Chain	Residue
C	GLU244
C	PRO364
C	MET366
C	TRP374
C	TYR423
C	LEU493
C	VAL494

site_id	AD3
Number of Residues	8
Details	binding site for residue GOL C 504

Chain	Residue
C	PRO126
C	LYS289
C	VAL291
C	TYR477
C	LEU478
C	TRP481
C	LYS482
C	CYS483

site_id	AD4
Number of Residues	27
Details	binding site for residue MYA D 501

Chain	Residue
D	TYR117
D	GLN118
D	PHE119
D	TRP120
D	ASN179
D	TYR180
D	ASN246
D	PHE247
D	LEU248
D	CYS249
D	VAL250
D	ARG255
D	SER256
D	LYS257
D	ARG258
D	VAL259
D	ALA260
D	PRO261
D	THR268
D	PHE277
D	TYR281
D	THR282
D	LEU287
D	TYR479
D	MG502
D	HOH633
D	HOH671

site_id	AD5
Number of Residues	6
Details	binding site for residue MG D 502

Chain	Residue
D	LEU254
D	SER256
D	LYS257
D	ARG258
D	VAL259
D	MYA501

site_id	AD6
Number of Residues	5
Details	binding site for residue GOL D 503

Chain	Residue
D	GLU244
D	TRP374
D	TYR423
D	VAL494
D	HOH626

site_id	AD7
Number of Residues	7
Details	binding site for residue GOL D 504

Chain	Residue
D	PRO126
D	LYS289
D	VAL291
D	LEU478
D	TRP481
D	LYS482
D	CYS483

site_id	AD8
Number of Residues	5
Details	binding site for residue GOL D 505

Chain	Residue
D	THR122
D	GLU139
D	LYS142
D	ARG265
D	ALA390

Functional Information from PROSITE/UniProt

site_id	PS00975
Number of Residues	9
Details	NMT_1 Myristoyl-CoA:protein N-myristoyltransferase signature 1. EINFLCvHK

Chain	Residue	Details
A	GLU244-LYS252

site_id	PS00976
Number of Residues	7
Details	NMT_2 Myristoyl-CoA:protein N-myristoyltransferase signature 2. KFGiGDG

Chain	Residue	Details
A	LYS466-GLY472

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:25255805, ECO:0000269\|PubMed:32111831, ECO:0000269\|Ref.19

Chain	Residue	Details
A	LEU198
C	LEU338
C	ARG339
C	PRO340
D	LEU198
D	LEU338
D	ARG339
D	PRO340
A	LEU338
A	ARG339
A	PRO340
B	LEU198
B	LEU338
B	ARG339
B	PRO340
C	LEU198

site_id	SWS_FT_FI2
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:25255805, ECO:0000269\|PubMed:32103017, ECO:0000269\|PubMed:32111831, ECO:0000269\|Ref.19

Chain	Residue	Details
A	TRP199
B	ALA336
C	TRP199
C	ALA200
C	ARG328
C	PRO330
C	ALA336
D	TRP199
D	ALA200
D	ARG328
D	PRO330
A	ALA200
D	ALA336
A	ARG328
A	PRO330
A	ALA336
B	TRP199
B	ALA200
B	ARG328
B	PRO330

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:32103017

Chain	Residue	Details
A	TYR327
B	TYR327
C	TYR327
D	TYR327

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:25255805, ECO:0000269\|Ref.19

Chain	Residue	Details
A	LEU329
B	LEU329
C	LEU329
D	LEU329

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:O70310

Chain	Residue	Details
A	GLU111
B	GLU111
C	GLU111
D	GLU111

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:16964243, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	LYS127
B	LYS127
C	LYS127
D	LYS127

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	LEU163
B	LEU163
C	LEU163
D	LEU163

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