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6SVM

Crystal structure of human GFAT-1 in complex with Glucose-6-Phosphate, L-Glu, and UDP-GalNAc

Functional Information from GO Data
ChainGOidnamespacecontents
A0004360molecular_functionglutamine-fructose-6-phosphate transaminase (isomerizing) activity
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
A1901137biological_processcarbohydrate derivative biosynthetic process
B0004360molecular_functionglutamine-fructose-6-phosphate transaminase (isomerizing) activity
B0097367molecular_functioncarbohydrate derivative binding
B1901135biological_processcarbohydrate derivative metabolic process
B1901137biological_processcarbohydrate derivative biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue G6Q A 701
ChainResidue
ACYS374
ASER474
ALYS558
AGLU561
AHOH802
AHOH809
AHOH831
BHIS577
AGLY375
ATHR376
ASER377
ASER421
AGLN422
ASER423
ATHR426
AALA473

site_idAC2
Number of Residues11
Detailsbinding site for residue GLU A 702
ChainResidue
ACYS2
AARG95
ATRP96
ATHR98
AHIS99
AHIS108
AHIS122
AASN123
AGLY124
AASP148
ATHR149

site_idAC3
Number of Residues15
Detailsbinding site for residue UD2 A 703
ChainResidue
AGLN310
AARG343
AGLY355
AGLY445
ATHR447
ASER455
ATHR458
ACYS460
AGLY461
AVAL462
AHIS463
AMG704
AHOH811
BTYR535
BHIS536

site_idAC4
Number of Residues4
Detailsbinding site for residue MG A 704
ChainResidue
ASER455
AARG456
ATHR458
AUD2703

site_idAC5
Number of Residues14
Detailsbinding site for residue G6Q B 701
ChainResidue
AHIS577
BCYS374
BGLY375
BTHR376
BSER377
BSER421
BGLN422
BSER423
BTHR426
BALA473
BSER474
BLYS558
BGLU561
BHOH808

site_idAC6
Number of Residues12
Detailsbinding site for residue UD2 B 702
ChainResidue
BARG343
BGLY354
BGLY355
BGLY445
BTHR447
BSER455
BTHR458
BCYS460
BGLY461
BVAL462
BHIS463
BMG703

site_idAC7
Number of Residues4
Detailsbinding site for residue MG B 703
ChainResidue
BSER455
BARG456
BTHR458
BUD2702

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues278
DetailsDomain: {"description":"SIS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00797","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues282
DetailsDomain: {"description":"SIS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00797","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"For GATase activity","evidences":[{"source":"UniProtKB","id":"P14742","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19059404","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZJ4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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