Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6JQ9

Crystal structure of a lyase from Alteromonas sp.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0005576cellular_componentextracellular region
B0005886cellular_componentplasma membrane
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 601
ChainResidue
AASP212
AASP222
ALYS224
AHOH709
AHOH919
AHOH935

site_idAC2
Number of Residues7
Detailsbinding site for residue CA A 602
ChainResidue
AHOH766
AHOH824
AHOH913
AHOH920
AASN323
AASP326
APHE328

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 603
ChainResidue
AHIS377
ATHR378
AALA379
ASER382
AARG412
AHOH717

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 604
ChainResidue
AARG137
AHIS167
AARG177
APHE178
AHOH810

site_idAC5
Number of Residues7
Detailsbinding site for residue CA B 601
ChainResidue
BASN323
BASP326
BPHE328
BHOH726
BHOH747
BHOH832
BHOH942

site_idAC6
Number of Residues5
Detailsbinding site for residue CA B 602
ChainResidue
BASP212
BASP222
BLYS224
BHOH771
BHOH1008

site_idAC7
Number of Residues7
Detailsbinding site for residue SO4 B 603
ChainResidue
BHIS377
BTHR378
BALA379
BSER382
BARG412
BHOH842
BHOH893

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:29382716
ChainResidueDetails
AHIS146
BHIS146

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:29382716
ChainResidueDetails
ASER145
AHIS384
BSER145
BASP212
BASP222
BLYS224
BTYR303
BARG320
BASN323
BASP326
BPHE328
AASP212
BHIS384
AASP222
ALYS224
ATYR303
AARG320
AASN323
AASP326
APHE328

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Neutralizes the sugar carboxylate group at subsite +1 => ECO:0000305|PubMed:29382716
ChainResidueDetails
AARG259
BARG259

220113

PDB entries from 2024-05-22

PDB statisticsPDBj update infoContact PDBjnumon