Structure of PDB 3la4 Chain A

Receptor sequence
>3la4A (length=837) Species: 3823 (Canavalia ensiformis) [Search protein sequence]
MKLSPREVEKLGLHNAGYLAQKRLARGVRLNYTEAVALIASQIMEYARDG
EKTVAQLMCLGQHLLGRRQVLPAVPHLLNAVQVEATFPDGTKLVTVHDPI
SRENGELQEALFGSLLPVPSLDKFAEDNRIPGEILCEDECLTLNIGRKAV
ILKVTSKGDRPIQVGSHYHFIEVNPYLTFDRRKAYGMRLNIAAGTAVRFE
PGDCKSVTLVSIEGNKVIRGGNAIADGPVNETNLEAAMHAVRSKGFGHEE
EKDASEGFTKEDPNCPFNTFIHRKEYANKYGPTTGDKIRLGDTNLLAEIE
KDYALYGDECVFGGGKVIRDGMGQSCGHPPAISLDTVITNAVIIDYTGII
KADIGIKDGLIASIGKAGNPDIMNGVFSNMIIGANTEVIAGEGLIVTAGA
IDCHVHYICPQLVYEAISSGITTLVGGGTGPAAGTRATTCTPSPTQMRLM
LQSTDDLPLNFGFTGKGSSSKPDELHEIIKAGAMGLKLHEDWGSTPAAID
NCLTIAEHHDIQINIHTDTLNEAGFVEHSIAAFKGRTIHTYHSEGAGGGH
APDIIKVCGIKNVLPSSTNPTRPLTSNTIDEHLDMLMVCHHLDREIPEDL
AFAHSRIRKKTIAAEDVLNDIGAISIISSDSQAMGRVGEVISRTWQTADK
MKAQTGPLKCDSSDNDNFRIRRYIAKYTINPAIANGFSQYVGSVEVGKLA
DLVMWKPSFFGTKPEMVIKGGMVAWADIGDPNASIPTPEPVKMRPMYGTL
GKAGGALSIAFVSKAALDQRVNVLYGLNKRVEAVSNVRKLTKLDMKLNDA
LPEITVDPESYTVKADGKLLCVSEATTVPLSRNYFLF
3D structure
PDB3la4 Crystal structure of the first plant urease from jack bean: 83 years of journey from its first crystal to molecular structure
ChainA
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H407 H409 K490 H492 D494 H519 H545 H593 R609 D633
Catalytic site (residue number reindexed from 1) H404 H406 K487 H489 D491 H516 H542 H590 R606 D630
Enzyme Commision number 3.5.1.5: urease.
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 NI A H407 H409 K490 D633 H404 H406 K487 D630
BS02 NI A K490 H519 H545 K487 H516 H542
BS03 PO4 A H407 H409 A440 K490 H519 H545 D633 A636 H404 H406 A437 K487 H516 H542 D630 A633
BS04 PO4 A E493 D494 H519 H593 R609 E490 D491 H516 H590 R606
Gene Ontology
Molecular Function
GO:0009039 urease activity
GO:0016151 nickel cation binding
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0046872 metal ion binding
GO:0090729 toxin activity
Biological Process
GO:0035821 modulation of process of another organism
GO:0043419 urea catabolic process
Cellular Component
GO:0035550 urease complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3la4, PDBe:3la4, PDBj:3la4
PDBsum3la4
PubMed20471401
UniProtP07374|UREA_CANEN Urease

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