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2DXW

Crystal structure of Glu54 to Lys mutant of Diphthine synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004164molecular_functiondiphthine synthase activity
A0008168molecular_functionmethyltransferase activity
A0016740molecular_functiontransferase activity
A0017183biological_processprotein histidyl modification to diphthamide
A0032259biological_processmethylation
B0004164molecular_functiondiphthine synthase activity
B0008168molecular_functionmethyltransferase activity
B0016740molecular_functiontransferase activity
B0017183biological_processprotein histidyl modification to diphthamide
B0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1301
ChainResidue
BARG46
BHIS126
BTYR128
BHIS243
BHOH1575
BHOH1760

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 1302
ChainResidue
BHIS243
BHOH1537
BHOH1554
BHOH1632
BARG46
BLYS129
BLYS241

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1303
ChainResidue
AARG60
AHOH1604
AHOH1609

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1304
ChainResidue
ASER211
ALEU212
AASN213

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1305
ChainResidue
BPRO257
BARG258
BHOH1744
BHOH1768

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1306
ChainResidue
APRO257
AARG258
AHOH1595

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1307
ChainResidue
BARG60
BALA91
BTHR92
BTHR93
BHOH1594

site_idAC8
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SAH A 1300
ChainResidue
ALEU10
ATHR36
ASER37
AASP87
AVAL90
ASER115
AILE116
APHE165
ALEU166
ALEU206
AARG208
AALA209
APRO233
AHIS234
AHOH1515
AHOH1558
AHOH1566

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MES A 1501
ChainResidue
APHE34
AMET39
ATHR42
ATHR43
ALEU44
AVAL57
AHOH1710

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MES B 1502
ChainResidue
BASP200
BTYR220
BLYS222
BGLU259

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1401
ChainResidue
BLEU38
BMET39
BTHR42
BTHR43
BLEU44
BARG173

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1402
ChainResidue
ATYR128
AHIS243
BASN66
BLYS132
BHOH1634

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1403
ChainResidue
ATHR43
AARG46
AHOH1690
AHOH1715

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1404
ChainResidue
ATYR128
BGLU61
BLEU65
BALA134
BTHR135
BPHE165
BHOH1642
BHOH1660

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01084","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18391406","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of diphthine synthase from Pyrococcus horikoshii OT3.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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