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6H94

T16A variant of beta-phosphoglucomutase from Lactococcus lactis with phosphate and TRIS bound in an open conformer to 1.5 A.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0008801molecular_functionbeta-phosphoglucomutase activity
A0016853molecular_functionisomerase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 301
ChainResidue
AASP8
AASP10
AGLU169
AASP170
AHOH525

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 302
ChainResidue
AMET1
AASP137
ATRP216

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 303
ChainResidue
AGLY182
ATRP216
ALYS219
ASER163

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO A 304
ChainResidue
ALYS117
AASN118
AVAL160
AHOH409
AHOH410
AHOH489

site_idAC5
Number of Residues9
Detailsbinding site for residue PO4 A 305
ChainResidue
AARG49
ALYS117
ATRS306
AHOH434
AHOH445
AHOH446
AHOH456
AHOH489
AHOH501

site_idAC6
Number of Residues10
Detailsbinding site for residue TRS A 306
ChainResidue
AHIS20
ATRP24
ALEU44
AVAL47
AARG49
ALYS76
APO4305
AHOH420
AHOH504
AHOH517

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:15996095, ECO:0000305|PubMed:19154134
ChainResidueDetails
AASP8

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15996095, ECO:0000305|PubMed:19154134
ChainResidueDetails
AASP10

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12081483, ECO:0000269|PubMed:12637673, ECO:0000269|PubMed:15826149, ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:20164409, ECO:0007744|PDB:1LVH, ECO:0007744|PDB:1O03, ECO:0007744|PDB:1O08, ECO:0007744|PDB:1Z4N, ECO:0007744|PDB:1Z4O, ECO:0007744|PDB:1ZOL, ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6, ECO:0007744|PDB:2WHE
ChainResidueDetails
AASP8
AASP10
AASP170

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20164409, ECO:0000305|PubMed:12637673, ECO:0007744|PDB:1O03, ECO:0007744|PDB:1O08, ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6
ChainResidueDetails
AGLY46
AVAL47

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20164409, ECO:0000305|PubMed:12637673, ECO:0000305|PubMed:15826149, ECO:0007744|PDB:1O03, ECO:0007744|PDB:1O08, ECO:0007744|PDB:1Z4N, ECO:0007744|PDB:1Z4O, ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6
ChainResidueDetails
AARG49
ASER116
ALYS117
AASN118

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groups
ChainResidueDetails
ASER114
ALYS145

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: 4-aspartylphosphate => ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:19154134
ChainResidueDetails
AASP8

Catalytic Information from CSA
site_idMCSA1
Number of Residues10
DetailsM-CSA 206
ChainResidueDetails
AASP8metal ligand, nucleofuge, nucleophile
AASP170metal ligand
ALEU9electrostatic stabiliser, hydrogen bond donor
AASP10metal ligand, proton acceptor, proton donor
AALA16electrostatic stabiliser
ALYS45electrostatic stabiliser
ASER114electrostatic stabiliser, hydrogen bond donor
AALA115electrostatic stabiliser, hydrogen bond donor
ALYS145electrostatic stabiliser, hydrogen bond donor
AGLU169metal ligand

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PDB entries from 2024-11-06

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