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2A14

Crystal Structure of Human Indolethylamine N-methyltransferase with SAH

Functional Information from GO Data
ChainGOidnamespacecontents
A0004790molecular_functionthioether S-methyltransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008168molecular_functionmethyltransferase activity
A0008170molecular_functionN-methyltransferase activity
A0009308biological_processamine metabolic process
A0009636biological_processresponse to toxic substance
A0030748molecular_functionamine N-methyltransferase activity
A0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2003
ChainResidue
AARG200
AGLU217
ALYS218
AASN250
AARG258
AHOH4093
AHOH4234

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAH A 4001
ChainResidue
AGLY63
ASER64
AGLY65
ATHR67
ATYR69
AASP85
APHE86
ATHR87
AASN90
ACYS141
AASP142
AVAL143
AHIS144
ALEU163
ALEU164
AALA165
AALA169
AHOH4050
AHOH4064
ATYR20
ATYR25

Functional Information from PROSITE/UniProt
site_idPS01100
Number of Residues17
DetailsNNMT_PNMT_TEMT NNMT/PNMT/TEMT family of methyltransferases signature. LIDIGSGPTIYQVLAAC
ChainResidueDetails
ALEU59-CYS75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ATYR20
ATYR25
AGLY63
ATYR69
AASP85
AASN90
AASP142
ALEU163

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P40936
ChainResidueDetails
ALYS13
ALYS96

224201

PDB entries from 2024-08-28

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