Structure of PDB 4l78 Chain A

Receptor sequence

>4l78A (length=1285) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2)

GLVPRGSHMMEILRGSPALSAFRINKLLARFQAANLQVHNIYAEYVHFAD
LNAPLNDSEQAQLTRLLQYGPALSSHTPAGKLLLVTPRPGTISPWSSKAT
DIAHNCGLQQVDRLERGVAYYIEASTLTAEQWRQVAAELHDRMMETVFSS
LTDAEKLFIHHQPAPVSSVDLLGEGRQALIDANLRLGLALAEDEIDYLQE
AFTKLGRNPNDIELYMFAQANSEHCRHKIFNADWIIDGKPQPKSLFKMIK
NTFETTPDYVLSAYKDNAAVMEGSAVGRYFADHNTGRYDFHQEPAHILMK
VETHNHPTAISPWPGAATGSGGEIRDEGATGRGAKPKAGLVGFSVSNLRI
PGFEQPWEEDFGKPERIVTALDIMTEGPLGGAAFNNEFGRPALTGYFRTY
EEKVNSHNGEELRGYHKPIMLAGGIGNIRADHVQKGEIVVGAKLIVLGGP
AMNIGDFASVQRDNPEMERRCQEVIDRCWQLGDANPILFIHDVGAGGLSN
AMPELVSDGGRGGKFELRDILSDEPGMSPLEIWCNESQERYVLAVAADQL
PLFDELCKRERAPYAVIGDATEEQHLSLHDNHFDNQPIDLPLDVLLGKTP
KMTRDVQTLKAKGDALNRADITIADAVKRVLHLPTVAEKTFLVTIGDRTV
TGMVARDQMVGPWQVPVADCAVTTASLDSYYGEAMSIGERAPVALLDFAA
SARLAVGEALTNIAATQIGDIKRIKLSANWMAAAGHPGEDAGLYDAVKAV
GEELCPQLGLTIPVGKDSMSMKTRWQEGNEQREMTSPLSLVISAFARVED
VRHTLTPQLSTEDNALLLIDLGKGHNALGATALAQVYRQLGDKPADVRDV
AQLKGFYDAMQALVAARKLLAWHDRSDGGLLVTLAEMAFAGHCGVQVDIA
ALGDDHLAALFNEELGGVIQVRAEDRDAVEALLAQYGLADCVHYLGQALA
GDRFVITANDQTVFSESRTTLRVWWAETTWQMQRLRDNPQCADQEHEAKA
NDTDPGLNVKLSFDINEDIAAPYIATGARPKVAVLREQGVNSHVEMAAAF
HRAGFDAIDVHMSDLLGGRIGLGNFHALVACGGFSYGDVLGAGEGWAKSI
LFNHRVRDEFETFFHRPQTLALGVCNGCQMMSNLRELIPGSELWPRFVRN
HSDRFEARFSLVEVTQSPSLLLQGMVGSQMPIAVSHGEGRVEVRDDAHLA
ALESKGLVALRYVDNFGKVTETYPANPNGSPNGITAVTTENGRVTIMMPH
PEAVFRTVANSWHPENWGEDSPWMRIFRNARKQLG

3D structure

• PDB: 4l78 Importance of hydrophobic cavities in allosteric regulation of formylglycinamide synthetase: insight from xenon trapping and statistical coupling analysis
• Chain: A
• Resolution: 2.18 Å

Enzymatic activity

• Enzyme Commision number: 6.3.5.3: phosphoribosylformylglycinamidine synthase.

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	ADP	A	V333 T386 G387 Y388 K649 L652 Q668 P676 A678 N722	V341 T394 G395 Y396 K639 L642 Q658 P666 A668 N712
BS02	MG	A	D679 N722 D884	D669 N712 D874
BS03	XE	A	F1060 L1130 A1131 L1132	F1050 L1120 A1121 L1122
BS04	XE	A	I417 A681 V682 T683 E693 A694 M695	I425 A671 V672 T673 E683 A684 M685
BS05	XE	A	F194 F209	F202 F217
BS06	XE	A	K878 A938 V939	K868 A928 V929
BS07	XE	A	E3 L5 H39 F40 A41	E11 L13 H47 F48 A49

Gene Ontology

Molecular Function

• GO:0004642 phosphoribosylformylglycinamidine synthase activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006164 purine nucleotide biosynthetic process
• GO:0006189 'de novo' IMP biosynthetic process
• GO:0006541 glutamine metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:4l78, PDBe:4l78, PDBj:4l78
• PDBsum: 4l78
• PubMed: 24223728
• UniProt: P74881|PUR4_SALTY Phosphoribosylformylglycinamidine synthase (Gene Name=purL)