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2HR8

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 Residues2
DetailsBINDING SITE FOR RESIDUE PT A 901
ChainResidue
AMET1
AGLU77

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PT A 902
ChainResidue
AMET174

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PT A 903
ChainResidue
AMET220

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PT B 904
ChainResidue
BMET1
BASP79

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PT B 905
ChainResidue
BMET174

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SAH A 801
ChainResidue
ASER37
AASP87
AVAL90
ATHR92
ASER115
AILE116
APHE165
ALEU166
AARG208
AALA209
APRO233
AHIS234
ALEU10
ATHR36

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 2024-07-17

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