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4GIK

Crystal Structure of Pseudouridine Monophosphate Glycosidase/Linear R5P Adduct

Functional Information from GO Data
ChainGOidnamespacecontents
A0001522biological_processpseudouridine synthesis
A0004730molecular_functionpseudouridylate synthase activity
A0005737cellular_componentcytoplasm
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016829molecular_functionlyase activity
A0030145molecular_functionmanganese ion binding
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0046113biological_processnucleobase catabolic process
A0046872molecular_functionmetal ion binding
B0001522biological_processpseudouridine synthesis
B0004730molecular_functionpseudouridylate synthase activity
B0005737cellular_componentcytoplasm
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016829molecular_functionlyase activity
B0030145molecular_functionmanganese ion binding
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0046113biological_processnucleobase catabolic process
B0046872molecular_functionmetal ion binding
C0001522biological_processpseudouridine synthesis
C0004730molecular_functionpseudouridylate synthase activity
C0005737cellular_componentcytoplasm
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0016829molecular_functionlyase activity
C0030145molecular_functionmanganese ion binding
C0032991cellular_componentprotein-containing complex
C0042802molecular_functionidentical protein binding
C0046113biological_processnucleobase catabolic process
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE R5P A 401
ChainResidue
AGLU31
ATHR270
AHOH511
AHOH515
AHOH529
AHOH535
AHOH621
AHOH623
AHOH627
AHOH645
ATHR33
ALYS93
ATHR112
AVAL113
AGLY132
ASER147
AASP149
ALYS166

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 402
ChainResidue
AASP145
AHOH620
AHOH622
AHOH623
AHOH645
CHOH553

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE R5P B 401
ChainResidue
BGLU31
BLYS93
BTHR112
BVAL113
BGLY132
BSER147
BASP149
BLYS166
BTHR270
BHOH503
BHOH508
BHOH526
BHOH534
BHOH550
BHOH600
BHOH601
BHOH618

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 402
ChainResidue
AHOH624
AHOH625
BASP145
BHOH599
BHOH601
BHOH618

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE R5P C 401
ChainResidue
CGLU31
CTHR33
CLYS93
CVAL113
CGLY132
CSER147
CASP149
CLYS166
CTHR270
CHOH505
CHOH512
CHOH536
CHOH539
CHOH550
CHOH552
CHOH556

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN C 402
ChainResidue
BHOH598
CASP145
CHOH549
CHOH550
CHOH551
CHOH552

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01876, ECO:0000303|PubMed:23066817
ChainResidueDetails
AGLU31
BGLU31
CGLU31

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01876, ECO:0000303|PubMed:23066817
ChainResidueDetails
ALYS166
BLYS166
CLYS166

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01876, ECO:0000269|PubMed:23066817
ChainResidueDetails
ALYS93
CVAL113
CASP145
CSER147
AVAL113
AASP145
ASER147
BLYS93
BVAL113
BASP145
BSER147
CLYS93

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PDB entries from 2024-10-30

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