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

3FVQ

Crystal structure of the nucleotide binding domain FbpC complexed with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006826biological_processiron ion transport
A0015408molecular_functionABC-type ferric iron transporter activity
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0034755biological_processiron ion transmembrane transport
A0098655biological_processmonoatomic cation transmembrane transport
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0006826biological_processiron ion transport
B0015408molecular_functionABC-type ferric iron transporter activity
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0034755biological_processiron ion transmembrane transport
B0098655biological_processmonoatomic cation transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ATP A 401
ChainResidue
APHE14
ATHR45
AGLN87
ACA360
AHOH368
AHOH385
AHOH391
AHOH399
AHOH428
BARG134
BGLU138
ATHR17
BSER140
BGLY141
BGLY142
BGLN143
BHOH416
AVAL19
ASER39
AGLY40
ACYS41
AGLY42
ALYS43
ATHR44

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 360
ChainResidue
ATHR44
AGLN87
AHOH367
AHOH385
AATP401

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA A 361
ChainResidue
BHIS288

site_idAC4
Number of Residues27
DetailsBINDING SITE FOR RESIDUE ATP B 360
ChainResidue
AARG134
AGLU138
ASER140
AGLY141
AGLY142
AGLN143
AHOH421
BPHE14
BGLN15
BTHR17
BVAL19
BSER39
BGLY40
BCYS41
BGLY42
BLYS43
BTHR44
BTHR45
BGLN87
BCA361
BHOH408
BHOH415
BHOH475
BHOH487
BHOH551
BHOH583
BHOH640

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 361
ChainResidue
BTHR44
BGLN87
BATP360
BHOH372
BHOH408

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQQQRAALARAL
ChainResidueDetails
ALEU139-LEU153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01706
ChainResidueDetails
AGLY37
BGLY37

225158

PDB entries from 2024-09-18

PDB statisticsPDBj update infoContact PDBjnumon