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3RSM

Crystal structure of S108C mutant of PMM/PGM

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004614molecular_functionphosphoglucomutase activity
A0004615molecular_functionphosphomannomutase activity
A0005975biological_processcarbohydrate metabolic process
A0008152biological_processmetabolic process
A0009103biological_processlipopolysaccharide biosynthetic process
A0009243biological_processO antigen biosynthetic process
A0009244biological_processlipopolysaccharide core region biosynthetic process
A0009298biological_processGDP-mannose biosynthetic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0042121biological_processalginic acid biosynthetic process
A0046872molecular_functionmetal ion binding
A0071704biological_processorganic substance metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 500
ChainResidue
AASP242
AASP244
AASP246
APO4464

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 464
ChainResidue
AARG247
AHIS329
AZN500
ACYS108
ALYS118
AASP242
AASP244
AASP246

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:23517223
ChainResidueDetails
AARG20

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Non-phosphorylated intermediate => ECO:0000305|PubMed:11839312, ECO:0000305|PubMed:14725765, ECO:0000305|PubMed:16880541
ChainResidueDetails
ACYS108

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:23517223
ChainResidueDetails
AHIS329

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:14725765, ECO:0007744|PDB:1PCJ
ChainResidueDetails
ATYR17
AHIS308
AGLU325
AARG421

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: via phosphate group => ECO:0000269|PubMed:11839312, ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:23517223
ChainResidueDetails
ACYS108

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11839312, ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:24403075
ChainResidueDetails
AASP242
AASP244
AASP246

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:18690721, ECO:0007744|PDB:1P5D, ECO:0007744|PDB:3BKQ
ChainResidueDetails
ALYS285

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11839312, ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541
ChainResidueDetails
ACYS108

Catalytic Information from CSA
site_idMCSA1
Number of Residues9
DetailsM-CSA 194
ChainResidueDetails
AARG20electrostatic stabiliser, hydrogen bond donor
ACYS108metal ligand, nucleofuge, nucleophile
AHIS109electrostatic stabiliser, hydrogen bond donor
ALYS118electrostatic stabiliser, hydrogen bond donor
AASP242metal ligand
AASP244metal ligand
AASP246metal ligand
AARG247electrostatic stabiliser, hydrogen bond donor
AHIS329electrostatic stabiliser, polar interaction

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PDB entries from 2024-04-24

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