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5VVE

Crystal structure of phosphoglycerate mutase from Naegleria fowleri

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
B0003824molecular_functioncatalytic activity
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue GOL A 300
ChainResidue
AHIS10
AHOH598
ASER13
AASN16
ATHR22
AARG61
AGLU88
AHIS183
AHOH450
AHOH514

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 301
ChainResidue
ATRP67
ALYS82
BTRP67
BVAL80
BLYS82

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 302
ChainResidue
ALYS64
ATRP67
AGLU71
AHOH419
BLYS64

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 303
ChainResidue
AGLU14
AGLY28
ALEU29
ALYS64

site_idAC5
Number of Residues9
Detailsbinding site for residue GOL B 301
ChainResidue
BHIS10
BSER13
BASN16
BTHR22
BARG61
BGLU88
BHIS183
BHOH499
BHOH517

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO B 302
ChainResidue
AHOH403
BGLY28
BLEU29
BLYS64

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO B 303
ChainResidue
BLYS4
BGLU47
BGLY48
BTYR49
BHOH455

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEsEwN
ChainResidueDetails
ALEU7-ASN16

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PDB entries from 2024-07-24

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