Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2Q4R

Ensemble refinement of the protein crystal structure of human phosphomannomutase 2 (PMM2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004615molecular_functionphosphomannomutase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006013biological_processmannose metabolic process
A0006486biological_processprotein glycosylation
A0006487biological_processprotein N-linked glycosylation
A0009298biological_processGDP-mannose biosynthetic process
A0016853molecular_functionisomerase activity
A0043025cellular_componentneuronal cell body
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 300
ChainResidue
ATYR106
ALYS109
ALYS156
AGLY402

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GLY A 400
ChainResidue
AARG21
ATYR201
ALYS202
AARG225
AHOH480

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GLY A 401
ChainResidue
APHE221
ATHR222
AASP223
ATHR226
AGLY228

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GLY A 402
ChainResidue
ASER105
ATYR106
ALYS109
AEDO300

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q92871
ChainResidueDetails
AASP12

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q92871
ChainResidueDetails
AASP14

site_idSWS_FT_FI3
Number of Residues11
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q92871
ChainResidueDetails
AASP12
AASP223
ATHR226
AASP14
AARG21
AARG123
AARG134
AARG141
ASER179
AASP181
APHE221

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P31353
ChainResidueDetails
AASP209

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2M7
ChainResidueDetails
ALYS149

220760

PDB entries from 2024-06-05

PDB statisticsPDBj update infoContact PDBjnumon