Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6SK3

C-terminal HsNMT1 deltaC3 truncation in complex with both MyrCoA and GNCFSKPR substrates

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 Residues8
Detailsbinding site for residue GOL A 501
ChainResidue
APRO126
ALYS289
AVAL291
ATYR477
ALEU478
ATRP481
ALYS482
ACYS483

site_idAC2
Number of Residues28
Detailsbinding site for residue MYA A 502
ChainResidue
AGLN118
APHE119
ATRP120
AASN179
ATYR180
AVAL181
APHE247
ALEU248
ACYS249
AVAL250
AARG255
ASER256
ALYS257
AARG258
AVAL259
AALA260
APRO261
AILE264
ATHR268
AVAL271
APHE277
AALA279
ATYR281
ATHR282
ALEU287
ATYR479
CASN3
ATYR117

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL B 501
ChainResidue
BPRO126
BLYS289
BVAL291
BLEU478
BTRP481
BLYS482
BCYS483

site_idAC4
Number of Residues26
Detailsbinding site for residue MYA B 502
ChainResidue
BTYR117
BGLN118
BPHE119
BTRP120
BASN179
BTYR180
BVAL181
BILE245
BPHE247
BLEU248
BCYS249
BVAL250
BARG255
BSER256
BARG258
BVAL259
BALA260
BPRO261
BILE264
BTHR268
BALA279
BTHR282
BLEU287
BTYR479
BMG503
DASN3

site_idAC5
Number of Residues2
Detailsbinding site for residue MG B 503
ChainResidue
BSER116
BMYA502

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: BINDING => ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:32111831, ECO:0000269|Ref.19
ChainResidueDetails
AARG339
APRO340
BLEU198
BLEU338
BARG339
BPRO340
ALEU198
ALEU338

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:32111831, ECO:0000269|Ref.19
ChainResidueDetails
AARG328
APRO330
AALA336
BTRP199
BALA200
BARG328
BPRO330
BALA336
ATRP199
AALA200

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

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

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

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
ALYS127
BLYS127

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

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon