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4GIJ

Crystal Structure of Pseudouridine Monophosphate Glycosidase Complexed with Sulfate

Functional Information from GO Data
ChainGOidnamespacecontents
A0001522biological_processpseudouridine synthesis
A0004730molecular_functionpseudouridylate synthase activity
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
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
B0016787molecular_functionhydrolase activity
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
C0016787molecular_functionhydrolase activity
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 Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 400
ChainResidue
ALYS93
ASER147
ATHR270
AHOH524
AHOH566
AHOH657
AHOH658
CHOH526

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AGLY266
AHOH516
AHOH529
AHOH566
CHOH510
CHOH526
AASP145

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 400
ChainResidue
AHOH521
BLYS93
BSER147
BTHR270
BHOH506
BHOH511
BHOH542
BHOH568
BHOH607

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 401
ChainResidue
AHOH515
AHOH521
BASP145
BHOH503
BHOH509
BHOH511

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 400
ChainResidue
CSER147
CHOH514
CHOH516
CHOH529
CHOH574

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN C 401
ChainResidue
BHOH535
BHOH557
CASP145
CHOH514
CHOH534
CHOH580

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01876","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23066817","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01876","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23066817","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01876","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23066817","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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