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

4IZ9

Crystal structure of an acetate kinase from Mycobacterium avium bound to an unknown acid-ApCpp conjugate and manganese

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006082biological_processorganic acid metabolic process
A0006083biological_processacetate metabolic process
A0006085biological_processacetyl-CoA biosynthetic process
A0008776molecular_functionacetate kinase activity
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0016774molecular_functionphosphotransferase activity, carboxyl group as acceptor
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AGLU374
AAPC402
ASIN403
AHOH637
AHOH638
AHOH639

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE APC A 402
ChainResidue
AGLY200
AASN201
AASP272
APHE273
AARG274
AALA319
AGLY320
AILE321
AASN324
AASP325
AMN401
ASIN403
AHOH578
AHOH634
AHOH637
AHOH638
AHOH722
AHOH781
AASN15
ALYS22
AGLU105

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SIN A 403
ChainResidue
AARG81
AHIS170
AHIS198
AGLY200
AASN201
AGLY202
AMN401
AAPC402
AEDO404
AHOH639

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 404
ChainResidue
AARG81
AASP138
AHIS170
AMET218
APRO222
AARG231
ASIN403

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 405
ChainResidue
AALA150
ATHR151
AHOH648

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 406
ChainResidue
AGLN288
ASER292
ATHR295
AHOH533
AHOH705

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 407
ChainResidue
ALEU306
AGLY310
AHIS311
ATHR312
AGLU338
AHOH709

Functional Information from PROSITE/UniProt
site_idPS01075
Number of Residues12
DetailsACETATE_KINASE_1 Acetate and butyrate kinases family signature 1. VLvINsGSSSlK
ChainResidueDetails
AVAL11-LYS22

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00020
ChainResidueDetails
AASP138

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00020
ChainResidueDetails
AASN15
ALYS22
AARG81
AHIS198
AASP272
AGLY320
AGLU374

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00020
ChainResidueDetails
AHIS170
AARG231

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon