Structure of PDB 3ttf Chain A

Receptor sequence
>3ttfA (length=646) Species: 83334 (Escherichia coli O157:H7) [Search protein sequence]
QIVPDAATCPACLAEMNTPGERRYRYPFINCTHCGPRFTIIRAMPYDRPF
TVMAAFPLCPACDKEYRDPLDRRFHAQPVACPECGPYLEWVSHGEHAEQE
AALQAAIAQLKMGNIVAIKGIGGFHLACDARNSNAVATLRARKHRPAKPL
AVMLPVADGLPDAARQLLTTPAAPIVLVDKKYVPELCDDIAPGLNEVGVM
LPANPLQHLLLQELQCPLVMTSGNLSGKPPAISNEQALEDLQGIADGFLI
HNRDIVQRMDDSVVRESGEMLRRSRGYVPDALALPPGFKNVPPVLCLGAD
LKNTFCLVRGEQVVLSQHLGDLSDDGIQTQWREALRLMQNIYNFTPQYVV
HDAHPGYVSCQWASEMNLPTQTVLHHHAHAAACLAEHQWPLDGGDVIALT
LDGIGMGENGALWGGECLRVNYRECEHLGGLPAVALPGGDLAAKQPWRNL
LAQCLRFVPEWQNYPETASVAAANWSVLARAIERGINAPLASSCGRLFDA
VAAALGCAPATLSYEGEAACALEALAASCDGVTHPVTMPRVDNQLDLATF
WQQWLNWQAPVNQRAWAFHDALAQGFAALMREQATMRGITTLVFSGGVIH
NRLLRARLAHYLADFTLLFPQSLPAGDGGLSLGQGVIAAARWLAGE
3D structure
PDB3ttf Structure of Hydrogenase Maturation Protein HypF with Reaction Intermediates Shows Two Active Sites.
ChainA
Resolution1.92 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.1.7: acylphosphatase.
6.2.-.-
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 ZN A C109 C112 C134 C9 C12 C34
BS02 ZN A C162 C181 C184 C62 C81 C84
BS03 ZN A H475 H479 D502 D727 H375 H379 D402 D627
BS04 AMP A H479 D502 F598 E615 A619 E623 G697 V698 N701 G726 D727 H379 D402 F498 E515 A519 E523 G597 V598 N601 G626 D627
Gene Ontology
Molecular Function
GO:0003725 double-stranded RNA binding
GO:0008270 zinc ion binding
GO:0016743 carboxyl- or carbamoyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0046944 protein carbamoylation

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Molecular Function

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Biological Process
External links
PDB RCSB:3ttf, PDBe:3ttf, PDBj:3ttf
PDBsum3ttf
PubMed22153500
UniProtA0A0H3JHT3

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