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2P77

Crystal structure of TTHB049 from Thermus thermophilus HB8

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0016791molecular_functionphosphatase activity
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0016791molecular_functionphosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 2001
ChainResidue
AALA79
AGLU81
BALA79
BGLU81

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1001
ChainResidue
APHE120
AGLY123
ALEU124
AHOH1057
AHOH1111

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1002
ChainResidue
BPHE48
BPHE120
BGLY123
BLEU124
BHOH2014
BHOH2174

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1003
ChainResidue
AGLY101
ASER111
BSER65
BARG67
BHOH2060

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

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
AARG54
AHIS8
AHIS133
AGLU74

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
BARG54
BHIS8
BHIS133
BGLU74

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PDB entries from 2024-07-24

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