Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6EHJ

Human N-myristoyltransferase (NMT1) with Myristoyl-CoA and peptide bound

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue GOL A 501

Chain	Residue
A	GLU244
A	HOH673
A	PRO364
A	MET366
A	TRP374
A	PHE422
A	TYR423
A	VAL494
A	LEU495
A	GLN496

site_id	AC2
Number of Residues	8
Details	binding site for residue GOL A 502

Chain	Residue
A	PRO126
A	LYS289
A	PRO290
A	VAL291
A	LEU478
A	TRP481
A	LYS482
A	CYS483

site_id	AC3
Number of Residues	8
Details	binding site for residue SER A 505

Chain	Residue
A	VAL181
A	TYR296
A	GLN496
A	GLY504
A	ASN506
A	HOH671
A	HOH693
A	HOH698

site_id	AC4
Number of Residues	6
Details	binding site for residue ASN A 506

Chain	Residue
A	GLY284
A	TYR296
A	ASN473
A	SER505
A	LYS507
A	SER508

site_id	AC5
Number of Residues	7
Details	binding site for residue LYS A 507

Chain	Residue
A	VAL181
A	PHE190
A	TYR420
A	ASN506
A	SER508
A	HOH657
A	HOH681

site_id	AC6
Number of Residues	9
Details	binding site for residue SER A 508

Chain	Residue
A	TYR296
A	HIS298
A	GLY470
A	ASP471
A	GLY472
A	ASN506
A	LYS507
A	LYS509
A	HOH657

site_id	AC7
Number of Residues	7
Details	binding site for residue LYS A 509

Chain	Residue
A	ASP185
A	HIS298
A	GLY470
A	ASP471
A	SER508
A	PRO510
A	LYS511

site_id	AC8
Number of Residues	4
Details	binding site for residue PRO A 510

Chain	Residue
A	HIS298
A	PHE311
A	LYS509
A	LYS511

site_id	AC9
Number of Residues	7
Details	binding site for residue LYS A 511

Chain	Residue
A	ARG295
A	HIS313
A	ILE469
A	GLY470
A	LYS509
A	PRO510
A	HOH646

site_id	AD1
Number of Residues	12
Details	binding site for residue MYR A 512

Chain	Residue
A	TRP120
A	PHE247
A	LEU248
A	ILE264
A	THR268
A	PHE277
A	TYR281
A	THR282
A	TYR479
A	MYA503
A	GLY504
A	COA513

site_id	AD2
Number of Residues	22
Details	binding site for residue COA A 513

Chain	Residue
A	MYR512
A	ARG115
A	TYR117
A	GLN118
A	PHE119
A	TRP120
A	ASN179
A	TYR180
A	VAL181
A	LEU248
A	CYS249
A	VAL250
A	ARG255
A	SER256
A	ARG258
A	VAL259
A	ALA260
A	PRO261
A	THR282
A	LEU287
A	MYA503
A	GLY504

site_id	AD3
Number of Residues	6
Details	binding site for residue GOL B 501

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

site_id	AD4
Number of Residues	7
Details	binding site for residue GOL B 502

Chain	Residue
B	GLU244
B	TRP374
B	TYR423
B	LEU493
B	VAL494
B	LEU495
B	GLN496

site_id	AD5
Number of Residues	22
Details	binding site for residue COA B 503

Chain	Residue
B	ARG115
B	TYR117
B	GLN118
B	PHE119
B	TRP120
B	ASN179
B	TYR180
B	VAL181
B	LEU248
B	CYS249
B	VAL250
B	ARG255
B	SER256
B	ARG258
B	VAL259
B	ALA260
B	PRO261
B	THR282
B	LEU287
B	MYR504
B	GLY505
B	HOH603

site_id	AD6
Number of Residues	8
Details	binding site for residue SER B 506

Chain	Residue
B	VAL181
B	PHE190
B	TYR192
B	GLN496
B	GLY505
B	ASN507
B	HOH621
B	HOH638

site_id	AD7
Number of Residues	8
Details	binding site for residue ASN B 507

Chain	Residue
B	PHE190
B	TYR296
B	GLY472
B	ASN473
B	SER506
B	LYS508
B	SER509
B	HOH651

site_id	AD8
Number of Residues	10
Details	binding site for residue LYS B 508

Chain	Residue
B	GLU182
B	ASP183
B	PHE188
B	PHE190
B	TYR420
B	ASN507
B	SER509
B	HOH640
B	HOH650
B	HOH651

site_id	AD9
Number of Residues	8
Details	binding site for residue SER B 509

Chain	Residue
B	HIS298
B	GLY470
B	ASP471
B	GLY472
B	ASN507
B	LYS508
B	LYS510
B	HOH651

site_id	AE1
Number of Residues	9
Details	binding site for residue LYS B 510

Chain	Residue
B	ASP183
B	ASP184
B	ASP185
B	HIS298
B	GLY470
B	ASP471
B	SER509
B	PRO511
B	LYS512

site_id	AE2
Number of Residues	4
Details	binding site for residue PRO B 511

Chain	Residue
B	PHE311
B	ILE469
B	LYS510
B	LYS512

site_id	AE3
Number of Residues	3
Details	binding site for residue LYS B 512

Chain	Residue
B	ILE469
B	LYS510
B	PRO511

site_id	AE4
Number of Residues	30
Details	binding site for Di-peptide MYA A 503 and GLY A 504

Chain	Residue
A	ARG115
A	TYR117
A	GLN118
A	PHE119
A	TRP120
A	ASN179
A	TYR180
A	VAL181
A	ILE245
A	ASN246
A	PHE247
A	LEU248
A	CYS249
A	VAL250
A	ARG255
A	SER256
A	ARG258
A	VAL259
A	ALA260
A	PRO261
A	THR268
A	VAL271
A	PHE277
A	THR282
A	LEU287
A	TYR479
A	SER505
A	MYR512
A	COA513
A	HOH635

site_id	AE5
Number of Residues	15
Details	binding site for Di-peptide MYR B 504 and GLY B 505

Chain	Residue
B	TRP120
B	TYR180
B	ILE245
B	ASN246
B	PHE247
B	LEU248
B	THR268
B	VAL271
B	PHE277
B	ALA279
B	THR282
B	TYR479
B	COA503
B	SER506
B	HOH617

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	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25255805","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32111831","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human type-I N-myristoyltransferase with bound myristoyl-CoA and inhibitor DDD90055.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25255805","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32103017","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32111831","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human type-I N-myristoyltransferase with bound myristoyl-CoA and inhibitor DDD90055.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32103017","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25255805","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human type-I N-myristoyltransferase with bound myristoyl-CoA and inhibitor DDD90055.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

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