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

1Y10

Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state

Functional Information from GO Data
ChainGOidnamespacecontents
A0004016molecular_functionadenylate cyclase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0006171biological_processcAMP biosynthetic process
A0008289molecular_functionlipid binding
A0009190biological_processcyclic nucleotide biosynthetic process
A0009268biological_processresponse to pH
A0010855molecular_functionadenylate cyclase inhibitor activity
A0016829molecular_functionlyase activity
A0030145molecular_functionmanganese ion binding
A0035556biological_processintracellular signal transduction
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
B0004016molecular_functionadenylate cyclase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0006171biological_processcAMP biosynthetic process
B0008289molecular_functionlipid binding
B0009190biological_processcyclic nucleotide biosynthetic process
B0009268biological_processresponse to pH
B0010855molecular_functionadenylate cyclase inhibitor activity
B0016829molecular_functionlyase activity
B0030145molecular_functionmanganese ion binding
B0035556biological_processintracellular signal transduction
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
C0004016molecular_functionadenylate cyclase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0006171biological_processcAMP biosynthetic process
C0008289molecular_functionlipid binding
C0009190biological_processcyclic nucleotide biosynthetic process
C0009268biological_processresponse to pH
C0010855molecular_functionadenylate cyclase inhibitor activity
C0016829molecular_functionlyase activity
C0030145molecular_functionmanganese ion binding
C0035556biological_processintracellular signal transduction
C0042803molecular_functionprotein homodimerization activity
C0046872molecular_functionmetal ion binding
D0004016molecular_functionadenylate cyclase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0006171biological_processcAMP biosynthetic process
D0008289molecular_functionlipid binding
D0009190biological_processcyclic nucleotide biosynthetic process
D0009268biological_processresponse to pH
D0010855molecular_functionadenylate cyclase inhibitor activity
D0016829molecular_functionlyase activity
D0030145molecular_functionmanganese ion binding
D0035556biological_processintracellular signal transduction
D0042803molecular_functionprotein homodimerization activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA C 604
ChainResidue
CASP265
CHOH690
DGLU136

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA D 605
ChainResidue
DASP222
DLEU223
DASP265

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 606
ChainResidue
BASP265
AHOH673
BASP222
BLEU223

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 607
ChainResidue
AASP222
ALEU223
AASP265
AARG298
AHOH669

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 608
ChainResidue
AGLU136
AHOH673
BASP222
BASP265
BHOH661

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 609
ChainResidue
AGLU44
AHOH624
AHOH653
DGLU44

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA D 610
ChainResidue
CHOH708
DGLU195

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA D 611
ChainResidue
DASN319

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 1PE A 601
ChainResidue
ALEU53
AMET154
BPHE117
BVAL130

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 1PE B 602
ChainResidue
AMET193
BMET145
BSER167
BHOH706

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 1PE D 603
ChainResidue
CPHE117
CVAL130
CMET193
DALA149
DLEU150
DHOH730

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:11839758
ChainResidueDetails
AASP222
AASP265
BASP222
BASP265
CASP222
CASP265
DASP222
DASP265

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALYS261
DLYS261
DARG298
DASP312
AARG298
AASP312
BLYS261
BARG298
BASP312
CLYS261
CARG298
CASP312

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609
ChainResidueDetails
ATHR2
BTHR2
CTHR2
DTHR2

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ab8
ChainResidueDetails
AARG323

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ab8
ChainResidueDetails
BARG323

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ab8
ChainResidueDetails
CARG323

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ab8
ChainResidueDetails
DARG323

222036

PDB entries from 2024-07-03

PDB statisticsPDBj update infoContact PDBjnumon