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2P9Y

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 Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1001
ChainResidue
AARG67
APHE120
AGLY123
AHOH1153

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1002
ChainResidue
BARG67
BTYR69
BPHE120
BGLY123
BLEU124
BHOH2085
BPHE48

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1003
ChainResidue
AGLY101
ASER111
BSER65
BPRO66
BARG67

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1004
ChainResidue
BGLU74
BLEU96
BPHE99
BPHE113
BGLY135
BHOH2095

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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