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6PAV

Structure of Human NMT1 with products CoA and myristoyl-lysine peptide with acetylated N-terminus

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 Residues15
Detailsbinding site for residue COA B 501
ChainResidue
BTYR117
BARG258
BALA260
BPRO261
BLEU287
BMYR504
BHOH624
BGLN118
BPHE119
BTRP120
BASN179
BLEU248
BVAL250
BARG255
BSER256

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL B 502
ChainResidue
BLYS289
BVAL291
BLEU478
BTRP481
BLYS482
BCYS483

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL B 503
ChainResidue
BGLU244
BPRO364
BTRP374
BTYR423
BLEU493
BVAL494

site_idAC4
Number of Residues9
Detailsbinding site for residue MYR B 504
ChainResidue
BASN246
BPHE247
BLEU248
BTHR268
BTYR281
BTHR282
BTYR479
BCOA501
DLYS3

site_idAC5
Number of Residues18
Detailsbinding site for residue COA A 501
ChainResidue
ATYR117
AGLN118
APHE119
ATRP120
AASN179
ATYR180
AVAL181
ALEU248
ACYS249
AVAL250
AARG255
ASER256
AARG258
AVAL259
AALA260
AILE264
AVAL285
CMYR101

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 502
ChainResidue
APRO126
ALYS289
AVAL291
ALEU478
ATRP481
ALYS482
ACYS483

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL A 503
ChainResidue
AGLU244
APRO364
ATYR423
ALEU493
AVAL494
AGLN496

site_idAC8
Number of Residues17
Detailsbinding site for Di-peptide MYR C 101 and LYS C 3
ChainResidue
ATRP120
ATYR180
AVAL181
APHE190
AILE245
AASN246
APHE247
ALEU248
ATHR268
AALA279
ATYR281
ATHR282
ATYR479
ACOA501
CGLY2
CVAL4
CHOH201

Functional Information from PROSITE/UniProt
site_idPS00975
Number of Residues9
DetailsNMT_1 Myristoyl-CoA:protein N-myristoyltransferase signature 1. EINFLCvHK
ChainResidueDetails
BGLU244-LYS252

site_idPS00976
Number of Residues7
DetailsNMT_2 Myristoyl-CoA:protein N-myristoyltransferase signature 2. KFGiGDG
ChainResidueDetails
BLYS466-GLY472

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsLIPID: N6-myristoyl lysine => ECO:0000269|PubMed:32103017
ChainResidueDetails
DLYS3
BLEU338
BARG339
BPRO340
ALEU198
ALEU338
AARG339
APRO340

site_idSWS_FT_FI2
Number of Residues1
DetailsLIPID: N6-myristoyl lysine => ECO:0000269|PubMed:32103017
ChainResidueDetails
CLYS3
AALA336
BALA200
BARG328
BPRO330
BALA336
ATRP199
AALA200
AARG328
APRO330

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:32103017
ChainResidueDetails
BTYR327
ATYR327

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:25255805, ECO:0000269|Ref.19
ChainResidueDetails
BLEU329
ALEU329

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O70310
ChainResidueDetails
BGLU111
AGLU111

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_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
ChainResidueDetails
BLYS127
ALYS127

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BLEU163
ALEU163

223532

PDB entries from 2024-08-07

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