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2P5C

Crystal structure of PH0725 from Pyrococcus horikoshii OT3

Functional Information from GO Data
ChainGOidnamespacecontents
A0004164molecular_functiondiphthine synthase activity
A0008168molecular_functionmethyltransferase activity
A0017183biological_processprotein histidyl modification to diphthamide
A0032259biological_processmethylation
B0004164molecular_functiondiphthine synthase activity
B0008168molecular_functionmethyltransferase activity
B0017183biological_processprotein histidyl modification to diphthamide
B0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SAH A 1301
ChainResidue
ALEU10
ALEU166
ALEU206
AARG208
AALA209
APRO233
AHIS234
AILE235
AHOH1322
AHOH1376
AHOH1401
ATHR36
AHOH1434
ASER37
AGLY86
AASP87
AVAL90
ASER115
AILE116
APHE165

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 401
ChainResidue
BASP200
BTYR220
BLYS222
BGLU259

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 402
ChainResidue
BLEU38
BMET39
BTHR42
BTHR43
BARG173
BHOH500

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 403
ChainResidue
ATYR128
BTHR92
BALA134
BTHR135
BHOH458
BHOH527

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01084, ECO:0000305|PubMed:18391406, ECO:0000305|Ref.4
ChainResidueDetails
ALEU10
BVAL90
BSER115
BLEU166
BALA209
BHIS234
AASP87
AVAL90
ASER115
ALEU166
AALA209
AHIS234
BLEU10
BASP87

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PDB entries from 2024-08-28

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