Structure of PDB 7aqp Chain A

Receptor sequence
>7aqpA (length=323) Species: 2026 (Thermoactinomyces vulgaris) [Search protein sequence]
DFPSYDSGYHNYNEMVNKINTVASNYPNIVKKFSIGKSYEGRELWAVKIS
DNVGTDENEPEVLYTALHHAREHLTVEMALYTLDLFTQNYNLDSRITNLV
NNREIYIVFNINPDGGEYDISSGSYKSWRKNRQPNSGSSYVGTDLNRNYG
YKWGCCGGSSGSPSSETYRGRSAFSAPETAAMRDFINSRVVGGKQQIKTL
ITFHTYSELIQYPYGYTYTDVPSDMTQDDFNVFKTMANTMAQTNGYTPQQ
SSDSYITDGDMSDWAYGQHKIFAFTFEMYPTSYNPGFYPPDEVIGRETSR
NKEAVLYVAEKADCPYSVIGKSC
3D structure
PDB7aqp T262S, A251S, L254S, L211Q mutant of carboxypeptidase T from Thermoactinomyces vulgaris
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H69 E72 R129 H204 E277
Catalytic site (residue number reindexed from 1) H69 E72 R129 H204 E277
Enzyme Commision number 3.4.17.18: carboxypeptidase T.
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 H69 E72 H204 H69 E72 H204
BS02 CA A S7 Y9 E14 S7 Y9 E14
BS03 CA A S50 D51 E57 E59 S50 D51 E57 E59
BS04 CA A D56 E57 E61 E104 D56 E57 E61 E104
BS05 CA A Y5 D291 E292 Y5 D291 E292
Gene Ontology
Molecular Function
GO:0004181 metallocarboxypeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:7aqp, PDBe:7aqp, PDBj:7aqp
PDBsum7aqp
PubMed
UniProtP29068|CBPT_THEVU Carboxypeptidase T (Gene Name=cpt)

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