Home Research COVID-19 Services Publications People Teaching Job Opening News Forum Lab Only
Online Services

I-TASSER I-TASSER-MTD C-I-TASSER CR-I-TASSER QUARK C-QUARK LOMETS MUSTER CEthreader SEGMER DeepFold DeepFoldRNA FoldDesign COFACTOR COACH MetaGO TripletGO IonCom FG-MD ModRefiner REMO DEMO DEMO-EM SPRING COTH Threpp PEPPI BSpred ANGLOR EDock BSP-SLIM SAXSTER FUpred ThreaDom ThreaDomEx EvoDesign BindProf BindProfX SSIPe GPCR-I-TASSER MAGELLAN ResQ STRUM DAMpred

TM-score TM-align US-align MM-align RNA-align NW-align LS-align EDTSurf MVP MVP-Fit SPICKER HAAD PSSpred 3DRobot MR-REX I-TASSER-MR SVMSEQ NeBcon ResPRE TripletRes DeepPotential WDL-RF ATPbind DockRMSD DeepMSA FASPR EM-Refiner GPU-I-TASSER

BioLiP E. coli GLASS GPCR-HGmod GPCR-RD GPCR-EXP Tara-3D TM-fold DECOYS POTENTIAL RW/RWplus EvoEF HPSF THE-DB ADDRESS Alpaca-Antibody CASP7 CASP8 CASP9 CASP10 CASP11 CASP12 CASP13 CASP14

BioLiP

Structure of PDB 1gll Chain O

Receptor sequence
>1gllO (length=494) Species: 562 (Escherichia coli) [Search protein sequence]
EKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPME
IWATQSWTLVEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAI
VWQCRRTAEICEHLKRDGLEDYIRSNTGLVIDPYFSGTKVKWILDHVEGS
RERARRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHTLDWDD
KMLEVLDIPREMLPEVRRSSEVYGQTNIGTRIPISGIAGDQQAALFGQLC
VKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNYALEGA
VFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPY
WDPYARGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHA
LRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQ
NLDELQEKAVIEREFRPGIETTERNYRYAGWKKAVKRAMAWEEH
3D structure
PDB1gll Crystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion.
ChainO
Resolution3.0 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 2.7.1.30: glycerol kinase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ACP O T13 T14 G266 T267 G310 I313 Q314 A326 G411 N415 T12 T13 G261 T262 G305 I308 Q309 A321 G406 N410
BS02 GOL O R83 E84 Y135 D245 Q246 F270 R82 E83 Y134 D240 Q241 F265
Gene Ontology
Molecular Function
GO:0004370 glycerol kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016301 kinase activity
GO:0016773 phosphotransferase activity, alcohol group as acceptor
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006071 glycerol metabolic process
GO:0006072 glycerol-3-phosphate metabolic process
GO:0006974 DNA damage response
GO:0016310 phosphorylation
GO:0019563 glycerol catabolic process
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1gll, PDBe:1gll, PDBj:1gll
PDBsum1gll
PubMed10090737
UniProtP0A6F3|GLPK_ECOLI Glycerol kinase (Gene Name=glpK)

[Back to BioLiP]

zhanglabzhanggroup.org | +65-6601-1241 | Computing 1, 13 Computing Drive, Singapore 117417