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3D1O

Structure of the PTP-Like Phytase Expressed by Selenomonas Ruminantium at an Ionic Strength of 300 mM

Functional Information from GO Data
ChainGOidnamespacecontents
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
B0016311biological_processdephosphorylation
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 400
ChainResidue
ATYR239
APRO243
AGLN244
ALYS270
AHOH437
AHOH756
AHOH793

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 401
ChainResidue
BGLN244
BLYS270
BHOH458
BHOH579
BHOH635
BTYR239
BPRO243

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 402
ChainResidue
BTYR42
BARG310
BALA346
BHOH546

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 403
ChainResidue
BLYS83
BPHE289
BPHE294
BLYS297

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
ALYS83
APHE289
APHE294
AILE296
ALYS297
AHOH587

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. FHCeaGvgRTT
ChainResidueDetails
APHE250-THR260

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PDB entries from 2024-09-11

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