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5E1M

Crystal structure of NTMT1 in complex with PPKRIA peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006338biological_processchromatin remodeling
A0006480biological_processN-terminal protein amino acid methylation
A0007051biological_processspindle organization
A0007059biological_processchromosome segregation
A0008168molecular_functionmethyltransferase activity
A0008276molecular_functionprotein methyltransferase activity
A0018013biological_processN-terminal peptidyl-glycine methylation
A0018016biological_processN-terminal peptidyl-proline dimethylation
A0032259biological_processmethylation
A0035572biological_processN-terminal peptidyl-serine dimethylation
A0035573biological_processN-terminal peptidyl-serine trimethylation
A0042054molecular_functionhistone methyltransferase activity
A0071885molecular_functionN-terminal protein N-methyltransferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006338biological_processchromatin remodeling
B0006480biological_processN-terminal protein amino acid methylation
B0007051biological_processspindle organization
B0007059biological_processchromosome segregation
B0008168molecular_functionmethyltransferase activity
B0008276molecular_functionprotein methyltransferase activity
B0018013biological_processN-terminal peptidyl-glycine methylation
B0018016biological_processN-terminal peptidyl-proline dimethylation
B0032259biological_processmethylation
B0035572biological_processN-terminal peptidyl-serine dimethylation
B0035573biological_processN-terminal peptidyl-serine trimethylation
B0042054molecular_functionhistone methyltransferase activity
B0071885molecular_functionN-terminal protein N-methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue SAH A 301
ChainResidue
ATRP20
APHE96
AGLY118
ALEU119
AGLN120
AGLN135
ATRP136
AVAL137
AHIS140
AHOH434
AHOH498
AMET30
AHOH514
AGLY69
AGLY71
AARG74
AILE75
AASP91
AILE92
ATHR93

site_idAC2
Number of Residues11
Detailsbinding site for residue GOL A 302
ChainResidue
ATRP136
AVAL137
AILE138
AGLY139
AASP167
AASN168
ASER182
AVAL183
AHOH448
AHOH450
DPRO1

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 303
ChainResidue
AGLU86
AARG112
AHOH460
AHOH503
AHOH512
BARG46

site_idAC4
Number of Residues20
Detailsbinding site for residue SAH B 301
ChainResidue
BTRP20
BMET30
BGLY69
BGLY71
BARG74
BILE75
BASP91
BILE92
BTHR93
BPHE96
BCYS117
BGLY118
BLEU119
BGLN120
BGLN135
BTRP136
BVAL137
BHIS140
BHOH415
BHOH486

site_idAC5
Number of Residues12
Detailsbinding site for residue GOL B 302
ChainResidue
BTRP136
BVAL137
BILE138
BGLY139
BASP167
BASN168
BSER182
BVAL183
BCYS184
BHOH419
BHOH423
EPRO1

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:26543159, ECO:0000269|PubMed:26543161, ECO:0007744|PDB:2EX4, ECO:0007744|PDB:5CVD, ECO:0007744|PDB:5CVE, ECO:0007744|PDB:5E1D, ECO:0007744|PDB:5E1M, ECO:0007744|PDB:5E1O, ECO:0007744|PDB:5E2A, ECO:0007744|PDB:5E2B
ChainResidueDetails
AGLY69
BGLN135
AARG74
AASP91
ALEU119
AGLN135
BGLY69
BARG74
BASP91
BLEU119

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylthreonine; in N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed => ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
ATHR2
BTHR2

227344

PDB entries from 2024-11-13

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