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2O2X

Crystal structure of a putative had-like phosphatase (mll2559) from mesorhizobium loti at 1.50 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0034200molecular_functionD-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase activity
A0046872molecular_functionmetal ion binding
A0097171biological_processADP-L-glycero-beta-D-manno-heptose biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 218
ChainResidue
AARG57
APRO58
AGLN59
AALA150
AHOH359
AHOH533

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 219
ChainResidue
AASP44
ATHR45
AASP46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues13
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Stabilizes the phosphoryl group","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Contributes to substrate recognition","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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