3JTK

Crystal Structure of human type-I N-myristoyltransferase with bound myristoyl-CoA and inhibitor DDD90055

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	36
Details	BINDING SITE FOR RESIDUE MYA A 1001

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	VAL271
A	PHE277
A	ALA279
A	TYR281
A	THR282
A	LEU287
A	TYR479
A	HOH530
A	HOH532
A	HOH545
A	PHE119
A	HOH559
A	HOH584
A	HOH644
A	HOH688
A	HOH701
A	HOH712
A	HOH806
A	TRP120
A	ASN179
A	TYR180
A	VAL181
A	PHE247
A	LEU248

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site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE X55 A 1002

Chain	Residue
A	VAL181
A	GLU182
A	ASP183
A	PHE188
A	ARG189
A	PHE190
A	TYR296
A	HIS298
A	PHE311
A	SER405
A	LEU416
A	TYR420
A	ASN451
A	HOH572

---

site_id	AC3
Number of Residues	34
Details	BINDING SITE FOR RESIDUE MYA B 2001

Chain	Residue
B	HOH107
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	ARG258
B	VAL259
B	ALA260
B	PRO261
B	THR268
B	VAL271
B	PHE277
B	TYR281
B	THR282
B	LEU287
B	TYR479
B	HOH526
B	HOH581
B	HOH601
B	HOH649
B	HOH763
B	HOH775
B	HOH816
B	HOH821

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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

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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

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