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

5F13

Structure of Mn bound DUF89 from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006974biological_processDNA damage response
A0008150biological_processbiological_process
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0046872molecular_functionmetal ion binding
A0097023molecular_functionfructose 6-phosphate aldolase activity
A0103026molecular_functionfructose-1-phosphatase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006974biological_processDNA damage response
B0008150biological_processbiological_process
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0046872molecular_functionmetal ion binding
B0097023molecular_functionfructose 6-phosphate aldolase activity
B0103026molecular_functionfructose-1-phosphatase activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0006974biological_processDNA damage response
C0008150biological_processbiological_process
C0016787molecular_functionhydrolase activity
C0016791molecular_functionphosphatase activity
C0046872molecular_functionmetal ion binding
C0097023molecular_functionfructose 6-phosphate aldolase activity
C0103026molecular_functionfructose-1-phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 501
ChainResidue
AASP254
AASN255
AASP292
APO4502
AHOH632
AHOH636

site_idAC2
Number of Residues9
Detailsbinding site for residue PO4 A 502
ChainResidue
ALEU385
ALYS423
AMN501
APO4503
AHOH627
AHOH632
AASP254
AASN255
AASP384

site_idAC3
Number of Residues8
Detailsbinding site for residue PO4 A 503
ChainResidue
AGLU110
AASP384
ALEU385
AARG388
APO4502
AHOH611
AHOH615
AHOH649

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 504
ChainResidue
AHIS38
AARG135

site_idAC5
Number of Residues4
Detailsbinding site for residue CL A 505
ChainResidue
AHIS282
AGLU344
AASP345
ATRP348

site_idAC6
Number of Residues6
Detailsbinding site for residue MN B 501
ChainResidue
BASP254
BASN255
BASP292
BPO4502
BHOH608
BHOH628

site_idAC7
Number of Residues9
Detailsbinding site for residue PO4 B 502
ChainResidue
BASP254
BASN255
BASP384
BLEU385
BMN501
BPO4503
BHOH603
BHOH608
BHOH628

site_idAC8
Number of Residues6
Detailsbinding site for residue PO4 B 503
ChainResidue
BGLU110
BASP384
BLEU385
BARG388
BPO4502
BHOH601

site_idAC9
Number of Residues1
Detailsbinding site for residue CL B 504
ChainResidue
BHIS38

site_idAD1
Number of Residues6
Detailsbinding site for residue EDO B 505
ChainResidue
BARG248
BARG343
BASP372
CARG248
CARG343
CASP372

site_idAD2
Number of Residues6
Detailsbinding site for residue MN C 501
ChainResidue
CASP254
CASN255
CASP292
CPO4502
CHOH608
CHOH609

site_idAD3
Number of Residues9
Detailsbinding site for residue PO4 C 502
ChainResidue
CASP254
CASN255
CASP384
CLEU385
CLYS423
CMN501
CPO4503
CHOH608
CHOH609

site_idAD4
Number of Residues5
Detailsbinding site for residue PO4 C 503
ChainResidue
CGLU110
CASP384
CLEU385
CARG388
CPO4502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:27322068, ECO:0007744|PDB:3PT1
ChainResidueDetails
AARG23
CGLU110
CASP384
CLYS423
AGLU110
AASP384
ALYS423
BARG23
BGLU110
BASP384
BLYS423
CARG23

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:27322068, ECO:0007744|PDB:3PT1, ECO:0007744|PDB:5BY0
ChainResidueDetails
AASP254
AASN255
AASP292
BASP254
BASN255
BASP292
CASP254
CASN255
CASP292

224201

PDB entries from 2024-08-28

PDB statisticsPDBj update infoContact PDBjnumon