Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4C2Y

Human N-myristoyltransferase (NMT1) with Myristoyl-CoA co-factor

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	37
Details	BINDING SITE FOR RESIDUE MYA B 1497

Chain	Residue
B	ARG115
B	PHE247
B	LEU248
B	CYS249
B	VAL250
B	ARG255
B	SER256
B	LYS257
B	ARG258
B	VAL259
B	ALA260
B	TYR117
B	PRO261
B	THR268
B	VAL271
B	PHE277
B	TYR281
B	THR282
B	LEU287
B	TYR479
B	MG1498
B	HOH2004
B	GLN118
B	HOH2224
B	HOH2226
B	HOH2402
B	HOH2403
B	HOH2404
B	HOH2405
B	HOH2406
B	HOH2407
B	PHE119
B	TRP120
B	ASN179
B	TYR180
B	VAL181
B	ASN246

site_id	AC2
Number of Residues	37
Details	BINDING SITE FOR RESIDUE MYA A 1497

Chain	Residue
A	TYR117
A	GLN118
A	PHE119
A	TRP120
A	ASN179
A	TYR180
A	VAL181
A	PHE247
A	LEU248
A	CYS249
A	VAL250
A	ARG255
A	SER256
A	LYS257
A	ARG258
A	VAL259
A	ALA260
A	PRO261
A	THR268
A	VAL271
A	PHE277
A	GLN278
A	TYR281
A	THR282
A	LEU287
A	TYR479
A	MG1498
A	HOH2002
A	HOH2217
A	HOH2218
A	HOH2378
A	HOH2379
A	HOH2380
A	HOH2381
A	HOH2382
A	HOH2383
A	HOH2384

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1498

Chain	Residue
A	LEU254
A	SER256
A	LYS257
A	ARG258
A	VAL259
A	MYA1497

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 1498

Chain	Residue
B	LEU254
B	SER256
B	LYS257
B	ARG258
B	VAL259
B	MYA1497

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CIT B 1499

Chain	Residue
B	THR122
B	GLN123
B	PRO124
B	GLU139
B	LYS142
B	ARG265
B	ALA336
B	ASN389
B	ALA390
B	HOH2230
B	HOH2286
B	HOH2408

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CIT A 1499

Chain	Residue
A	GLN123
A	PRO124
A	GLU139
A	LYS142
A	ARG265
A	ALA336
A	ASN389
A	ALA390
A	HOH2222
A	HOH2273
A	HOH2274
A	HOH2385
A	HOH2386
A	THR122

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 1500

Chain	Residue
A	PRO126
A	LYS289
A	PRO290
A	VAL291
A	LEU478
A	TRP481
A	LYS482
A	CYS483
A	SER485
A	HOH2243

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1501

Chain	Residue
A	TYR296
A	TYR401
A	LEU403
A	LEU474
A	LEU495
A	GLN496
A	HOH2238

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1502

Chain	Residue
A	ASP183
A	PHE188
A	HOH2118
A	HOH2389

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL B 1500

Chain	Residue
B	PRO126
B	LYS289
B	PRO290
B	VAL291
B	TYR477
B	LEU478
B	TRP481
B	LYS482
B	CYS483
B	HOH2254

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 1501

Chain	Residue
B	ASN133
B	THR134
B	PRO149
B	TRP158
B	HOH2018
B	HOH2051
B	HOH2064
B	HOH2066

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 1502

Chain	Residue
B	TYR192
B	TYR296
B	TYR401
B	LEU403
B	LEU474
B	LEU495
B	GLN496
B	HOH2247
B	HOH2262

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 1503

Chain	Residue
A	PRO204
A	GLY205
A	GLU369
A	HOH2138
B	LEU207
B	GLN209
B	GLU274
B	HOH2411
B	HOH2412

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)