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1XI3

Thiamine phosphate pyrophosphorylase from Pyrococcus furiosus Pfu-1255191-001

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004789molecular_functionthiamine-phosphate diphosphorylase activity
A0005737cellular_componentcytoplasm
A0009228biological_processthiamine biosynthetic process
A0009229biological_processthiamine diphosphate biosynthetic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004789molecular_functionthiamine-phosphate diphosphorylase activity
B0005737cellular_componentcytoplasm
B0009228biological_processthiamine biosynthetic process
B0009229biological_processthiamine diphosphate biosynthetic process
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
ATHR132
AGLY161
AGLY162
AILE182
ASER183
AHOH411
AHOH428

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI B 302
ChainResidue
BGLU29
BGLU29
BGLU26
BGLU26

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE UNX B 401
ChainResidue
BSER183

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX B 402
ChainResidue
BGLN36
BARG38
BGLN83

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 403
ChainResidue
APRO19
AVAL21
AGLU22

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00097
ChainResidueDetails
ASER106
ATHR132
ALYS135
AGLY162
AILE182
BGLN36
BASP68
BASP69
BASP88
BSER106
BTHR132
BLYS135
BGLY162
BILE182
AGLN36
AASP68
AASP69
AASP88

218500

PDB entries from 2024-04-17

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