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3IWE

Crystal Structure of human type-I N-myristoyltransferase with bound myristoyl-CoA and inhibitor DDD85646

Functional Information from GO Data
ChainGOidnamespacecontents
A0004379molecular_functionglycylpeptide N-tetradecanoyltransferase activity
A0006499biological_processN-terminal protein myristoylation
B0004379molecular_functionglycylpeptide N-tetradecanoyltransferase activity
B0006499biological_processN-terminal protein myristoylation
Functional Information from PDB Data
site_idAC1
Number of Residues36
DetailsBINDING SITE FOR RESIDUE MYA A 1001
ChainResidue
AHOH75
APHE247
ALEU248
ACYS249
AVAL250
AARG255
ASER256
ALYS257
AARG258
AVAL259
AALA260
AHOH83
APRO261
ATHR268
AVAL271
APHE277
ATYR281
ATHR282
ALEU287
ATYR479
AHOH526
AHOH529
ATYR117
AHOH560
AHOH617
AHOH618
AHOH632
AHOH741
AHOH752
A6461002
AGLN118
APHE119
ATRP120
AASN179
ATYR180
AVAL181

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 646 A 1002
ChainResidue
AHOH2
AVAL181
AASP183
APHE188
APHE190
AASN246
AGLY284
ATYR296
AHIS298
APHE311
ASER405
ATYR420
AGLY472
AGLN496
AHOH547
AHOH753
AHOH760
AHOH970
AMYA1001

site_idAC3
Number of Residues37
DetailsBINDING SITE FOR RESIDUE MYA B 2001
ChainResidue
BHOH103
BTYR117
BGLN118
BPHE119
BTRP120
BASN179
BTYR180
BVAL181
BASN246
BPHE247
BLEU248
BCYS249
BVAL250
BARG255
BSER256
BLYS257
BARG258
BVAL259
BALA260
BPRO261
BTHR268
BPHE277
BTYR281
BTHR282
BLEU287
BTYR479
BHOH548
BHOH669
BHOH680
BHOH725
BHOH766
BHOH788
BHOH789
BHOH800
BHOH989
BHOH1010
B6462002

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 646 B 2002
ChainResidue
BTHR282
BGLY284
BTYR296
BHIS298
BPHE311
BSER405
BTYR420
BASP471
BGLN496
BHOH529
BHOH731
BHOH744
BHOH1068
BMYA2001
BHOH1
BTYR180
BVAL181
BASP183
BPHE188
BPHE190
BASN246

Functional Information from PROSITE/UniProt
site_idPS00975
Number of Residues9
DetailsNMT_1 Myristoyl-CoA:protein N-myristoyltransferase signature 1. EINFLCvHK
ChainResidueDetails
AGLU244-LYS252

site_idPS00976
Number of Residues7
DetailsNMT_2 Myristoyl-CoA:protein N-myristoyltransferase signature 2. KFGiGDG
ChainResidueDetails
ALYS466-GLY472

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding 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)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding 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)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32103017","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding 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)"]}}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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