Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3RY7

Crystal Structure of Sa239

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004747molecular_functionribokinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006014biological_processD-ribose metabolic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0019303biological_processD-ribose catabolic process
A0044281biological_processsmall molecule metabolic process
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 401
ChainResidue
AASN12
AASP14
AGLY41
AASN45
AALA97
AGLU142
AHOH418
AHOH480

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
AILE87
ALYS88
ALYS233
AASN234
AGOL403
AILE86

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
ALYS205
AASN209
ATHR232
ALYS233
AGLN235
AGOL402

Functional Information from PROSITE/UniProt
site_idPS00584
Number of Residues14
DetailsPFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTtAAGDtfiGAFV
ChainResidueDetails
AASP248-VAL261

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01987","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01987","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

PDB statisticsPDBj update infoContact PDBjnumon