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6E4B

The crystal structure of a putative alpha-ribazole-5'-P phosphatase from Escherichia coli str. K-12 substr. MG1655

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0009236biological_processcobalamin biosynthetic process
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0043755molecular_functionalpha-ribazole phosphatase activity
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0009236biological_processcobalamin biosynthetic process
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0043755molecular_functionalpha-ribazole phosphatase activity
C0003824molecular_functioncatalytic activity
C0005737cellular_componentcytoplasm
C0009236biological_processcobalamin biosynthetic process
C0016787molecular_functionhydrolase activity
C0016791molecular_functionphosphatase activity
C0043755molecular_functionalpha-ribazole phosphatase activity
D0003824molecular_functioncatalytic activity
D0005737cellular_componentcytoplasm
D0009236biological_processcobalamin biosynthetic process
D0016787molecular_functionhydrolase activity
D0016791molecular_functionphosphatase activity
D0043755molecular_functionalpha-ribazole phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CL A 301
ChainResidue
APRO24
ATHR25
AARG57

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 302
ChainResidue
AARG7
AASN14
AHOH410

site_idAC3
Number of Residues5
Detailsbinding site for residue 1PE A 303
ChainResidue
AGLN139
ALYS186
AILE132
AALA133
ASER136

site_idAC4
Number of Residues7
Detailsbinding site for residue 1PE A 304
ChainResidue
AGLU81
AMET82
APHE84
ACYS107
AMET168
ATRP169
AHOH430

site_idAC5
Number of Residues4
Detailsbinding site for residue CL B 301
ChainResidue
BPRO24
BTHR25
BGLU56
BARG57

site_idAC6
Number of Residues3
Detailsbinding site for residue GOL B 302
ChainResidue
BGLU81
BMET82
BTRP169

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEtQaN
ChainResidueDetails
ALEU5-ASN14

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000250|UniProtKB:P62707
ChainResidueDetails
AHIS8
BHIS8
CHIS8
DHIS8

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P62707
ChainResidueDetails
AGLU81
BGLU81
CGLU81
DGLU81

223532

PDB entries from 2024-08-07

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