Structure of PDB 3ttc Chain A

Receptor sequence

>3ttcA (length=646) Species: 83334 (Escherichia coli O157:H7)

QIVPDAATCPACLAEMNTPGERRYRYPFINCTHCGPRFTIIRAMPYDRPF
TVMAAFPLCPACDKEYRDPLDRRFHAQPVACPECGPYLEWVSHGEHAEQE
AALQAAIAQLKMGNIVAIKGIGGFHLACDARNSNAVATLRARKHRPAKPL
AVMLPVADGLPDAARQLLTTPAAPIVLVDKKYVPELCDDIAPGLNEVGVM
LPANPLQHLLLQELQCPLVMTSGNLSGKPPAISNEQALEDLQGIADGFLI
HNRDIVQRMDDSVVRESGEMLRRSRGYVPDALALPPGFKNVPPVLCLGAD
LKNTFCLVRGEQVVLSQHLGDLSDDGIQTQWREALRLMQNIYNFTPQYVV
HDAHPGYVSCQWASEMNLPTQTVLHHHAHAAACLAEHQWPLDGGDVIALT
LDGIGMGENGALWGGECLRVNYRECEHLGGLPAVALPGGDLAAKQPWRNL
LAQCLRFVPEWQNYPETASVAAANWSVLARAIERGINAPLASSCGRLFDA
VAAALGCAPATLSYEGEAACALEALAASCDGVTHPVTMPRVDNQLDLATF
WQQWLNWQAPVNQRAWAFHDALAQGFAALMREQATMRGITTLVFSGGVIH
NRLLRARLAHYLADFTLLFPQSLPAGDGGLSLGQGVIAAARWLAGE

3D structure

• PDB: 3ttc Structure of Hydrogenase Maturation Protein HypF with Reaction Intermediates Shows Two Active Sites.
• Chain: A
• Resolution: 1.86 Å

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 C131 C134	C9 C12 C31 C34
BS02	ZN	A	C159 C162 C181 C184	C59 C62 C81 C84
BS03	ZN	A	H475 H479 D502 D727	H375 H379 D402 D627
BS04	ADP	A	R245 K248 P249 A251 L277 E296 T321 S322 R372	R145 K148 P149 A151 L177 E196 T221 S222 R272	MOAD: Kd~4uM
BS05	ADP	A	H475 H479 D502 G503 I504 F598 E615 A619 G697 V698 N701 G726 D727	H375 H379 D402 G403 I404 F498 E515 A519 G597 V598 N601 G626 D627	MOAD: Kd~4uM

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

External links

• PDB: RCSB:3ttc, PDBe:3ttc, PDBj:3ttc
• PDBsum: 3ttc
• PubMed: 22153500
• UniProt: A0A0H3JHT3