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5NW7

Crystal structure of candida albicans phosphomannose isomerase in complex with inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000032biological_processcell wall mannoprotein biosynthetic process
A0004476molecular_functionmannose-6-phosphate isomerase activity
A0005575cellular_componentcellular_component
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006486biological_processprotein glycosylation
A0008270molecular_functionzinc ion binding
A0009298biological_processGDP-mannose biosynthetic process
A0016853molecular_functionisomerase activity
A0031505biological_processfungal-type cell wall organization
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 501
ChainResidue
AGLN111
AHIS113
AGLU138
AHIS285
A9C2502

site_idAC2
Number of Residues20
Detailsbinding site for residue 9C2 A 502
ChainResidue
ALEU108
ASER109
AGLN111
AHIS113
ALYS136
AGLU138
AHIS285
ATYR287
AGLU294
AARG304
ALYS310
AZN501
AHOH615
AHOH648
AHOH673
AHOH732
ATYR16
ATRP18
AGLU48
ALYS100

Functional Information from PROSITE/UniProt
site_idPS00965
Number of Residues9
DetailsPMI_I_1 Phosphomannose isomerase type I signature 1. YpDdNHKPE
ChainResidueDetails
ATYR130-GLU138

site_idPS00966
Number of Residues26
DetailsPMI_I_2 Phosphomannose isomerase type I signature 2. HAYIsGdiIEcMAaSDNvVRAGfTPK
ChainResidueDetails
AHIS285-LYS310

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:8180205
ChainResidueDetails
AARG304

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8612079
ChainResidueDetails
AGLN111
AHIS113
AGLU138
AHIS285

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Its modification inactivates the enzyme
ChainResidueDetails
ACYS150

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 880
ChainResidueDetails
ASER109electrostatic stabiliser
AGLN111activator, metal ligand
AHIS113metal ligand
ALYS136proton acceptor, proton donor
AGLU138metal ligand, modifies pKa
AHIS285metal ligand
AARG304electrostatic stabiliser
ALYS310electrostatic stabiliser

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PDB entries from 2024-05-29

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