Structure of PDB 1b7x Chain B

Receptor sequence

>1b7xB (length=246) Species: 9606 (Homo sapiens)

IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRYERNIEKISMLEKIYIHPRYNWRENLDRDIAL
MKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKEGQPSVL
QVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFV
MKSPFNNRWYQMGIVSWGEGCDRDGKIGFYTHVFRLKKWIQKVIDQ

3D structure

• PDB: 1b7x Unexpected crucial role of residue 225 in serine proteases.
• Chain: B
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H57 D102 E192 G193 D194 S195 G196
• Catalytic site (residue number reindexed from 1): H43 D97 E192 G193 D194 S195 G196
• Enzyme Commision number: 3.4.21.5: thrombin.

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	peptide	B	D21 E23 M26 P28 W29 D116 H119 P120 C122 L129C Y134 K135 R137 N159 K202 P204 N205 R206 W207	D6 E8 M11 P13 W14 D111 H114 P115 C117 L127 Y132 K133 R135 N154 K202 P204 N207 R208 W209
BS02	peptide	B	H57 W60D N98 L99 D189 A190 S195 S214 W215 G216	H43 W50 N93 L94 D189 A190 S195 S216 W217 G218

Gene Ontology

Molecular Function

• GO:0004252 serine-type endopeptidase activity
• GO:0005509 calcium ion binding

Biological Process

• GO:0006508 proteolysis
• GO:0007596 blood coagulation

External links

• PDB: RCSB:1b7x, PDBe:1b7x, PDBj:1b7x
• PDBsum: 1b7x
• PubMed: 10051558
• UniProt: P00734|THRB_HUMAN Prothrombin (Gene Name=F2)