Structure of PDB 5vbu Chain A Binding Site BS01

Receptor Information
>5vbu Chain A (length=442) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KLPPLAPGFLHLLQPDLPIYLLGLTQKFGPIYRLHLGLQDVVVLNSKRTI
EEAMVKKWADFAGRPEPLTYKLVSRNYPDLSLGDYSLLWKAHKKLTRSAL
LLGIRDSMEPVVEQLTQEFCERMRAQPGTPVAIEEEFSLLTCSIICYLTF
GDKIKDDNLMPAYYKCIQEVLKTWSHWSIQIVDVIPFLRFFPNPGLRRLK
QAIEKRDHIVEMQLRQHKESLVAGQWRDMMDYMLQGVAGQLLEGHVHMAA
VDLLIGGTETTANTLSWAVVFLLHHPEIQQRLQEELDHESRVPYKDRARL
PLLNATIAEVLRLRPVVPLALPHRTTRPSSISGYDIPEGTVIIPNLQGAH
LDETVWERPHEFWPDRFLEPGKNSRALAFGCGARVCLGEPLARLELFVVL
TRLLQAFTLLPSGDALPSLQPLPHCSVILKMQPFQVRLQPRG
Ligand information
Ligand IDHEM
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyKABFMIBPWCXCRK-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8C=C)C)c(C)c7C=C
ACDLabs 12.01C=1c3c(c(c4C=C5C(=C(C=6C=C7C(=C(C8=CC=2C(=C(C=1N=2[Fe](n34)(N5=6)N78)CCC(=O)O)C)\C=C)C)\C=C)C)C)CCC(=O)O
FormulaC34 H32 Fe N4 O4
NamePROTOPORPHYRIN IX CONTAINING FE;
HEME
ChEMBL
DrugBankDB18267
ZINC
PDB chain5vbu Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5vbu Functional analysis of human cytochrome P450 21A2 variants involved in congenital adrenal hyperplasia.
Resolution3.31 Å
Binding residue
(original residue number in PDB)		R92 S109 K121 G292 G293 T296 V360 H366 A421 F422 R427 C429 L430 G431
Binding residue
(residue number reindexed from 1)		R64 S81 K93 G256 G257 T260 V317 H323 A378 F379 R384 C386 L387 G388
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T296 F422 C429
Catalytic site (residue number reindexed from 1) T260 F379 C386
Enzyme Commision number 1.14.14.16: steroid 21-monooxygenase.
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0004509 steroid 21-monooxygenase activity
GO:0005496 steroid binding
GO:0005506 iron ion binding
GO:0008395 steroid hydroxylase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0103069 17-hydroxyprogesterone 21-hydroxylase activity
GO:0106309 progesterone 21-hydroxylase activity
Biological Process
GO:0006694 steroid biosynthetic process
GO:0006704 glucocorticoid biosynthetic process
GO:0006705 mineralocorticoid biosynthetic process
GO:0008202 steroid metabolic process
GO:0016125 sterol metabolic process
GO:0042445 hormone metabolic process
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5vbu, PDBe:5vbu, PDBj:5vbu
PDBsum5vbu
PubMed28539365
UniProtP08686|CP21A_HUMAN Steroid 21-hydroxylase (Gene Name=CYP21A2)

[Back to BioLiP]